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HEADER HYDROLASE 27-SEP-22 8B6S
TITLE X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7 FUSION TO THE
TITLE 2 GREEN FLUORESCENT PROTEIN GFP (CHEMOG1) LABELED WITH A CHLOROALKANE
TITLE 3 TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GREEN FLUORESCENT PROTEIN,HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: GFP, DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HALOTAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS 2 GREEN FLUORESCENT PROTEIN, GFP, FLUOROPHORE, TETRAMETHYLERHODAMINE,
KEYWDS 3 TMR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,L.HELLWEG,J.HIBLOT
REVDAT 1 26-JUL-23 8B6S 0
JRNL AUTH L.HELLWEG,A.EDENHOFER,L.BARCK,M.C.HUPPERTZ,M.S.FREI,
JRNL AUTH 2 M.TARNAWSKI,A.BERGNER,B.KOCH,K.JOHNSSON,J.HIBLOT
JRNL TITL A GENERAL METHOD FOR THE DEVELOPMENT OF MULTICOLOR
JRNL TITL 2 BIOSENSORS WITH LARGE DYNAMIC RANGES.
JRNL REF NAT.CHEM.BIOL. 2023
JRNL REFN ESSN 1552-4469
JRNL PMID 37291200
JRNL DOI 10.1038/S41589-023-01350-1
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 89842
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4492
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 46.1800 - 5.5900 0.97 2873 152 0.1540 0.1750
REMARK 3 2 5.5900 - 4.4400 0.96 2890 152 0.1403 0.1449
REMARK 3 3 4.4400 - 3.8800 0.97 2877 152 0.1374 0.1649
REMARK 3 4 3.8800 - 3.5200 0.96 2870 151 0.1624 0.1783
REMARK 3 5 3.5200 - 3.2700 0.96 2880 151 0.1685 0.1817
REMARK 3 6 3.2700 - 3.0800 0.96 2860 151 0.1689 0.2135
REMARK 3 7 3.0800 - 2.9200 0.96 2882 152 0.1805 0.1952
REMARK 3 8 2.9200 - 2.8000 0.96 2875 151 0.1858 0.2301
REMARK 3 9 2.8000 - 2.6900 0.96 2880 151 0.1871 0.2175
REMARK 3 10 2.6900 - 2.6000 0.95 2829 149 0.1836 0.2067
REMARK 3 11 2.6000 - 2.5100 0.95 2873 151 0.1826 0.2074
REMARK 3 12 2.5100 - 2.4400 0.95 2785 147 0.1833 0.2528
REMARK 3 13 2.4400 - 2.3800 0.95 2886 152 0.1798 0.2196
REMARK 3 14 2.3800 - 2.3200 0.96 2818 148 0.1786 0.2145
REMARK 3 15 2.3200 - 2.2700 0.95 2827 149 0.1742 0.2072
REMARK 3 16 2.2700 - 2.2200 0.95 2861 151 0.1729 0.2235
REMARK 3 17 2.2200 - 2.1800 0.95 2822 148 0.1753 0.2319
REMARK 3 18 2.1800 - 2.1300 0.96 2852 150 0.1776 0.2082
REMARK 3 19 2.1300 - 2.1000 0.96 2874 152 0.1821 0.2306
REMARK 3 20 2.1000 - 2.0600 0.94 2837 149 0.1849 0.2082
REMARK 3 21 2.0600 - 2.0300 0.95 2824 149 0.1835 0.2115
REMARK 3 22 2.0300 - 2.0000 0.95 2816 148 0.1856 0.2197
REMARK 3 23 2.0000 - 1.9700 0.94 2881 151 0.1857 0.2257
REMARK 3 24 1.9700 - 1.9400 0.95 2779 147 0.1846 0.2315
REMARK 3 25 1.9400 - 1.9100 0.94 2807 147 0.1964 0.2349
REMARK 3 26 1.9100 - 1.8900 0.94 2811 147 0.2074 0.2139
REMARK 3 27 1.8900 - 1.8600 0.94 2835 150 0.2349 0.2905
REMARK 3 28 1.8600 - 1.8400 0.94 2796 147 0.2736 0.2943
REMARK 3 29 1.8400 - 1.8200 0.94 2796 147 0.2992 0.3522
REMARK 3 30 1.8200 - 1.8000 0.95 2854 150 0.3264 0.3645
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) : 0.223
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.529
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.95
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.13
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 8664
REMARK 3 ANGLE : 1.094 11793
REMARK 3 CHIRALITY : 0.060 1250
REMARK 3 PLANARITY : 0.008 1602
REMARK 3 DIHEDRAL : 13.227 3221
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 8B6S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1292125782.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-21
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99996
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89852
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 95.3
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.120
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: 5Y2X, 1GFL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.085 M TRIS-HCL PH 8.5, 0.17 M SODIUM
REMARK 280 ACETATE, 15% (V/V) GLYCEROL, 27% (M/V) PEG 4000, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
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: 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 GLY A 1
REMARK 465 LYS A 2
REMARK 465 LEU A 230
REMARK 465 GLY A 231
REMARK 465 MET A 232
REMARK 465 ASP A 233
REMARK 465 GLU A 234
REMARK 465 LEU A 235
REMARK 465 TYR A 236
REMARK 465 SER A 530
REMARK 465 GLY A 531
REMARK 465 GLY B 1
REMARK 465 LYS B 2
REMARK 465 THR B 229
REMARK 465 LEU B 230
REMARK 465 GLY B 231
REMARK 465 MET B 232
REMARK 465 ASP B 233
REMARK 465 GLU B 234
REMARK 465 LEU B 235
REMARK 465 TYR B 236
REMARK 465 SER B 530
REMARK 465 GLY B 531
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 276 44.11 -105.64
REMARK 500 THR A 277 -158.84 -100.46
REMARK 500 GLU A 332 -73.81 -106.58
REMARK 500 ASP A 340 -132.82 50.85
REMARK 500 GLU A 364 65.88 39.05
REMARK 500 ARG A 387 47.52 -84.64
REMARK 500 ASP A 390 -73.98 -100.86
REMARK 500 VAL A 479 -69.88 -133.86
REMARK 500 LEU A 505 -97.34 -115.39
REMARK 500 PRO B 276 42.92 -107.38
REMARK 500 GLU B 332 -82.35 -103.51
REMARK 500 ASP B 340 -132.56 54.86
REMARK 500 GLU B 364 66.27 36.96
REMARK 500 ARG B 387 48.53 -87.42
REMARK 500 ASP B 390 -69.34 -102.44
REMARK 500 VAL B 479 -68.34 -134.79
REMARK 500 LEU B 505 -97.85 -115.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8B6R RELATED DB: PDB
REMARK 900 RELATED ID: 8B6T RELATED DB: PDB
DBREF 8B6S A 2 237 UNP P42212 GFP_AEQVI 3 238
DBREF 8B6S A 238 527 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 8B6S B 2 237 UNP P42212 GFP_AEQVI 3 238
DBREF 8B6S B 238 527 UNP P0A3G3 DHAA_RHOSO 4 293
SEQADV 8B6S GLY A 1 UNP P42212 EXPRESSION TAG
SEQADV 8B6S LEU A 63 UNP P42212 TYR 66 CONFLICT
SEQADV 8B6S CRO A 64 UNP P42212 GLY 67 CONFLICT
SEQADV 8B6S LEU A 230 UNP P42212 HIS 231 CONFLICT
SEQADV 8B6S VAL A 281 UNP P0A3G3 LEU 47 CONFLICT
SEQADV 8B6S THR A 292 UNP P0A3G3 SER 58 CONFLICT
SEQADV 8B6S GLY A 312 UNP P0A3G3 ASP 78 CONFLICT
SEQADV 8B6S PHE A 321 UNP P0A3G3 TYR 87 CONFLICT
SEQADV 8B6S MET A 322 UNP P0A3G3 LEU 88 CONFLICT
SEQADV 8B6S PHE A 362 UNP P0A3G3 CYS 128 CONFLICT
SEQADV 8B6S THR A 389 UNP P0A3G3 ALA 155 CONFLICT
SEQADV 8B6S LYS A 394 UNP P0A3G3 GLU 160 CONFLICT
SEQADV 8B6S VAL A 401 UNP P0A3G3 ALA 167 CONFLICT
SEQADV 8B6S THR A 406 UNP P0A3G3 ALA 172 CONFLICT
SEQADV 8B6S MET A 409 UNP P0A3G3 LYS 175 CONFLICT
SEQADV 8B6S GLY A 410 UNP P0A3G3 CYS 176 CONFLICT
SEQADV 8B6S ASN A 429 UNP P0A3G3 LYS 195 CONFLICT
SEQADV 8B6S GLU A 458 UNP P0A3G3 ALA 224 CONFLICT
SEQADV 8B6S ASP A 461 UNP P0A3G3 ASN 227 CONFLICT
SEQADV 8B6S LYS A 491 UNP P0A3G3 GLU 257 CONFLICT
SEQADV 8B6S ALA A 498 UNP P0A3G3 THR 264 CONFLICT
SEQADV 8B6S ASN A 506 UNP P0A3G3 HIS 272 CONFLICT
SEQADV 8B6S LEU A 507 UNP P0A3G3 TYR 273 CONFLICT
SEQADV 8B6S SER A 525 UNP P0A3G3 PRO 291 CONFLICT
SEQADV 8B6S THR A 526 UNP P0A3G3 ALA 292 CONFLICT
SEQADV 8B6S GLU A 528 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6S ILE A 529 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6S SER A 530 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6S GLY A 531 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6S GLY B 1 UNP P42212 EXPRESSION TAG
SEQADV 8B6S LEU B 63 UNP P42212 TYR 66 CONFLICT
SEQADV 8B6S CRO B 64 UNP P42212 GLY 67 CONFLICT
SEQADV 8B6S LEU B 230 UNP P42212 HIS 231 CONFLICT
SEQADV 8B6S VAL B 281 UNP P0A3G3 LEU 47 CONFLICT
SEQADV 8B6S THR B 292 UNP P0A3G3 SER 58 CONFLICT
SEQADV 8B6S GLY B 312 UNP P0A3G3 ASP 78 CONFLICT
SEQADV 8B6S PHE B 321 UNP P0A3G3 TYR 87 CONFLICT
SEQADV 8B6S MET B 322 UNP P0A3G3 LEU 88 CONFLICT
SEQADV 8B6S PHE B 362 UNP P0A3G3 CYS 128 CONFLICT
SEQADV 8B6S THR B 389 UNP P0A3G3 ALA 155 CONFLICT
SEQADV 8B6S LYS B 394 UNP P0A3G3 GLU 160 CONFLICT
SEQADV 8B6S VAL B 401 UNP P0A3G3 ALA 167 CONFLICT
SEQADV 8B6S THR B 406 UNP P0A3G3 ALA 172 CONFLICT
SEQADV 8B6S MET B 409 UNP P0A3G3 LYS 175 CONFLICT
SEQADV 8B6S GLY B 410 UNP P0A3G3 CYS 176 CONFLICT
SEQADV 8B6S ASN B 429 UNP P0A3G3 LYS 195 CONFLICT
SEQADV 8B6S GLU B 458 UNP P0A3G3 ALA 224 CONFLICT
SEQADV 8B6S ASP B 461 UNP P0A3G3 ASN 227 CONFLICT
SEQADV 8B6S LYS B 491 UNP P0A3G3 GLU 257 CONFLICT
SEQADV 8B6S ALA B 498 UNP P0A3G3 THR 264 CONFLICT
SEQADV 8B6S ASN B 506 UNP P0A3G3 HIS 272 CONFLICT
SEQADV 8B6S LEU B 507 UNP P0A3G3 TYR 273 CONFLICT
SEQADV 8B6S SER B 525 UNP P0A3G3 PRO 291 CONFLICT
SEQADV 8B6S THR B 526 UNP P0A3G3 ALA 292 CONFLICT
SEQADV 8B6S GLU B 528 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6S ILE B 529 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6S SER B 530 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6S GLY B 531 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 529 GLY LYS GLY GLU GLU LEU PHE THR GLY VAL VAL PRO ILE
SEQRES 2 A 529 LEU VAL GLU LEU ASP GLY ASP VAL ASN GLY HIS LYS PHE
SEQRES 3 A 529 SER VAL SER GLY GLU GLY GLU GLY ASP ALA THR TYR GLY
SEQRES 4 A 529 LYS LEU THR LEU LYS PHE ILE CYS THR THR GLY LYS LEU
SEQRES 5 A 529 PRO VAL PRO TRP PRO THR LEU VAL THR THR LEU CRO VAL
SEQRES 6 A 529 GLN CYS PHE SER ARG TYR PRO ASP HIS MET LYS GLN HIS
SEQRES 7 A 529 ASP PHE PHE LYS SER ALA MET PRO GLU GLY TYR VAL GLN
SEQRES 8 A 529 GLU ARG THR ILE PHE PHE LYS ASP ASP GLY ASN TYR LYS
SEQRES 9 A 529 THR ARG ALA GLU VAL LYS PHE GLU GLY ASP THR LEU VAL
SEQRES 10 A 529 ASN ARG ILE GLU LEU LYS GLY ILE ASP PHE LYS GLU ASP
SEQRES 11 A 529 GLY ASN ILE LEU GLY HIS LYS LEU GLU TYR ASN TYR ASN
SEQRES 12 A 529 SER HIS ASN VAL TYR ILE MET ALA ASP LYS GLN LYS ASN
SEQRES 13 A 529 GLY ILE LYS VAL ASN PHE LYS ILE ARG HIS ASN ILE GLU
SEQRES 14 A 529 ASP GLY SER VAL GLN LEU ALA ASP HIS TYR GLN GLN ASN
SEQRES 15 A 529 THR PRO ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP ASN
SEQRES 16 A 529 HIS TYR LEU SER THR GLN SER ALA LEU SER LYS ASP PRO
SEQRES 17 A 529 ASN GLU LYS ARG ASP HIS MET VAL LEU LEU GLU PHE VAL
SEQRES 18 A 529 THR ALA ALA GLY ILE THR LEU GLY MET ASP GLU LEU TYR
SEQRES 19 A 529 LYS ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 20 A 529 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 21 A 529 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 22 A 529 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 23 A 529 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 24 A 529 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 25 A 529 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 26 A 529 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 27 A 529 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 28 A 529 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 29 A 529 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 30 A 529 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 31 A 529 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 32 A 529 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 33 A 529 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 34 A 529 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 35 A 529 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 36 A 529 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 37 A 529 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 38 A 529 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 39 A 529 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 40 A 529 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 41 A 529 TRP LEU SER THR LEU GLU ILE SER GLY
SEQRES 1 B 529 GLY LYS GLY GLU GLU LEU PHE THR GLY VAL VAL PRO ILE
SEQRES 2 B 529 LEU VAL GLU LEU ASP GLY ASP VAL ASN GLY HIS LYS PHE
SEQRES 3 B 529 SER VAL SER GLY GLU GLY GLU GLY ASP ALA THR TYR GLY
SEQRES 4 B 529 LYS LEU THR LEU LYS PHE ILE CYS THR THR GLY LYS LEU
SEQRES 5 B 529 PRO VAL PRO TRP PRO THR LEU VAL THR THR LEU CRO VAL
SEQRES 6 B 529 GLN CYS PHE SER ARG TYR PRO ASP HIS MET LYS GLN HIS
SEQRES 7 B 529 ASP PHE PHE LYS SER ALA MET PRO GLU GLY TYR VAL GLN
SEQRES 8 B 529 GLU ARG THR ILE PHE PHE LYS ASP ASP GLY ASN TYR LYS
SEQRES 9 B 529 THR ARG ALA GLU VAL LYS PHE GLU GLY ASP THR LEU VAL
SEQRES 10 B 529 ASN ARG ILE GLU LEU LYS GLY ILE ASP PHE LYS GLU ASP
SEQRES 11 B 529 GLY ASN ILE LEU GLY HIS LYS LEU GLU TYR ASN TYR ASN
SEQRES 12 B 529 SER HIS ASN VAL TYR ILE MET ALA ASP LYS GLN LYS ASN
SEQRES 13 B 529 GLY ILE LYS VAL ASN PHE LYS ILE ARG HIS ASN ILE GLU
SEQRES 14 B 529 ASP GLY SER VAL GLN LEU ALA ASP HIS TYR GLN GLN ASN
SEQRES 15 B 529 THR PRO ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP ASN
SEQRES 16 B 529 HIS TYR LEU SER THR GLN SER ALA LEU SER LYS ASP PRO
SEQRES 17 B 529 ASN GLU LYS ARG ASP HIS MET VAL LEU LEU GLU PHE VAL
SEQRES 18 B 529 THR ALA ALA GLY ILE THR LEU GLY MET ASP GLU LEU TYR
SEQRES 19 B 529 LYS ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 20 B 529 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 21 B 529 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 22 B 529 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 23 B 529 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 24 B 529 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 25 B 529 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 26 B 529 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 27 B 529 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 28 B 529 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 29 B 529 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 30 B 529 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 31 B 529 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 32 B 529 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 33 B 529 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 34 B 529 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 35 B 529 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 36 B 529 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 37 B 529 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 38 B 529 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 39 B 529 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 40 B 529 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 41 B 529 TRP LEU SER THR LEU GLU ILE SER GLY
HET CRO A 64 22
HET CRO B 64 22
HET OEH A 601 44
HET CL A 602 1
HET GOL A 603 6
HET OEH B 601 44
HET CL B 602 1
HET GOL B 603 6
HETNAM CRO {2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-
HETNAM 2 CRO HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-
HETNAM 3 CRO YL}ACETIC ACID
HETNAM OEH [9-[2-CARBOXY-5-[2-[2-(6-CHLORANYLHEXOXY)
HETNAM 2 OEH ETHOXY]ETHYLCARBAMOYL]PHENYL]-6-(DIMETHYLAMINO)
HETNAM 3 OEH XANTHEN-3-YLIDENE]-DIMETHYL-AZANIUM
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN CRO PEPTIDE DERIVED CHROMOPHORE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 CRO 2(C15 H17 N3 O5)
FORMUL 3 OEH 2(C35 H43 CL N3 O6 1+)
FORMUL 4 CL 2(CL 1-)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 9 HOH *460(H2 O)
HELIX 1 AA1 GLY A 3 THR A 8 5 6
HELIX 2 AA2 PRO A 55 VAL A 60 5 6
HELIX 3 AA3 VAL A 67 SER A 71 5 5
HELIX 4 AA4 PRO A 74 HIS A 80 5 7
HELIX 5 AA5 ASP A 81 ALA A 86 1 6
HELIX 6 AA6 LYS A 155 ASN A 158 5 4
HELIX 7 AA7 SER A 278 ARG A 283 5 6
HELIX 8 AA8 ILE A 285 ALA A 290 1 6
HELIX 9 AA9 PHE A 314 LEU A 329 1 16
HELIX 10 AB1 ASP A 340 ASN A 353 1 14
HELIX 11 AB2 THR A 371 TRP A 375 5 5
HELIX 12 AB3 PRO A 376 ARG A 387 1 12
HELIX 13 AB4 ASP A 390 ILE A 397 1 8
HELIX 14 AB5 ASN A 400 GLY A 405 1 6
HELIX 15 AB6 LEU A 407 VAL A 411 5 5
HELIX 16 AB7 THR A 416 GLU A 425 1 10
HELIX 17 AB8 PRO A 426 LEU A 428 5 3
HELIX 18 AB9 ASN A 429 ASP A 432 5 4
HELIX 19 AC1 ARG A 433 LEU A 443 1 11
HELIX 20 AC2 PRO A 449 SER A 466 1 18
HELIX 21 AC3 PRO A 482 LEU A 493 1 12
HELIX 22 AC4 LEU A 507 ASN A 512 1 6
HELIX 23 AC5 ASN A 512 THR A 526 1 15
HELIX 24 AC6 GLY B 3 THR B 8 5 6
HELIX 25 AC7 ALA B 36 TYR B 38 5 3
HELIX 26 AC8 PRO B 55 VAL B 60 5 6
HELIX 27 AC9 VAL B 67 SER B 71 5 5
HELIX 28 AD1 PRO B 74 HIS B 80 5 7
HELIX 29 AD2 ASP B 81 ALA B 86 1 6
HELIX 30 AD3 SER B 278 ARG B 283 5 6
HELIX 31 AD4 ILE B 285 ALA B 290 1 6
HELIX 32 AD5 PHE B 314 LEU B 329 1 16
HELIX 33 AD6 ASP B 340 ASN B 353 1 14
HELIX 34 AD7 THR B 371 TRP B 375 5 5
HELIX 35 AD8 PRO B 376 PHE B 378 5 3
HELIX 36 AD9 ALA B 379 ARG B 387 1 9
HELIX 37 AE1 ASP B 390 ILE B 397 1 8
HELIX 38 AE2 ASN B 400 GLY B 405 1 6
HELIX 39 AE3 LEU B 407 VAL B 411 5 5
HELIX 40 AE4 THR B 416 GLU B 425 1 10
HELIX 41 AE5 PRO B 426 LEU B 428 5 3
HELIX 42 AE6 ASN B 429 ASP B 432 5 4
HELIX 43 AE7 ARG B 433 LEU B 443 1 11
HELIX 44 AE8 PRO B 449 SER B 466 1 18
HELIX 45 AE9 PRO B 482 LEU B 493 1 12
HELIX 46 AF1 LEU B 507 ASN B 512 1 6
HELIX 47 AF2 ASN B 512 THR B 526 1 15
SHEET 1 AA112 VAL A 10 VAL A 21 0
SHEET 2 AA112 HIS A 24 ASP A 35 -1 O PHE A 26 N GLY A 19
SHEET 3 AA112 LYS A 40 CYS A 47 -1 O ILE A 46 N SER A 29
SHEET 4 AA112 HIS A 216 ALA A 226 -1 O MET A 217 N PHE A 45
SHEET 5 AA112 HIS A 198 SER A 207 -1 N ALA A 205 O LEU A 220
SHEET 6 AA112 ASN A 148 ASP A 154 -1 N ILE A 151 O HIS A 198
SHEET 7 AA112 GLY A 159 ASN A 169 -1 O GLY A 159 N ASP A 154
SHEET 8 AA112 VAL A 175 PRO A 186 -1 O HIS A 180 N PHE A 164
SHEET 9 AA112 TYR A 91 PHE A 99 -1 N VAL A 92 O THR A 185
SHEET 10 AA112 ASN A 104 GLU A 114 -1 O TYR A 105 N ILE A 97
SHEET 11 AA112 THR A 117 ILE A 127 -1 O VAL A 119 N LYS A 112
SHEET 12 AA112 VAL A 10 VAL A 21 1 N ASP A 20 O GLY A 126
SHEET 1 AA2 8 HIS A 247 VAL A 251 0
SHEET 2 AA2 8 GLU A 254 VAL A 261 -1 O GLU A 254 N VAL A 251
SHEET 3 AA2 8 CYS A 295 PRO A 298 -1 O CYS A 295 N VAL A 261
SHEET 4 AA2 8 VAL A 269 LEU A 272 1 N PHE A 271 O ILE A 296
SHEET 5 AA2 8 VAL A 334 HIS A 339 1 O VAL A 335 N LEU A 270
SHEET 6 AA2 8 VAL A 357 MET A 363 1 O ALA A 361 N LEU A 336
SHEET 7 AA2 8 LYS A 470 PRO A 477 1 O LEU A 471 N PHE A 362
SHEET 8 AA2 8 CYS A 496 GLY A 504 1 O ILE A 501 N TRP A 474
SHEET 1 AA312 VAL B 11 VAL B 21 0
SHEET 2 AA312 HIS B 24 ASP B 35 -1 O PHE B 26 N GLY B 19
SHEET 3 AA312 LYS B 40 CYS B 47 -1 O ILE B 46 N SER B 29
SHEET 4 AA312 HIS B 216 ALA B 226 -1 O LEU B 219 N LEU B 43
SHEET 5 AA312 HIS B 198 SER B 207 -1 N TYR B 199 O ALA B 226
SHEET 6 AA312 ASN B 148 ASP B 154 -1 N ILE B 151 O HIS B 198
SHEET 7 AA312 GLY B 159 ASN B 169 -1 O GLY B 159 N ASP B 154
SHEET 8 AA312 VAL B 175 PRO B 186 -1 O GLN B 176 N HIS B 168
SHEET 9 AA312 TYR B 91 PHE B 99 -1 N VAL B 92 O THR B 185
SHEET 10 AA312 ASN B 104 GLU B 114 -1 O TYR B 105 N ILE B 97
SHEET 11 AA312 THR B 117 ILE B 127 -1 O VAL B 119 N LYS B 112
SHEET 12 AA312 VAL B 11 VAL B 21 1 N ASP B 20 O GLY B 126
SHEET 1 AA4 8 HIS B 247 VAL B 251 0
SHEET 2 AA4 8 GLU B 254 VAL B 261 -1 O GLU B 254 N VAL B 251
SHEET 3 AA4 8 CYS B 295 PRO B 298 -1 O CYS B 295 N VAL B 261
SHEET 4 AA4 8 VAL B 269 LEU B 272 1 N PHE B 271 O ILE B 296
SHEET 5 AA4 8 VAL B 334 HIS B 339 1 O VAL B 335 N LEU B 270
SHEET 6 AA4 8 VAL B 357 MET B 363 1 O ALA B 361 N LEU B 336
SHEET 7 AA4 8 LYS B 470 PRO B 477 1 O LEU B 471 N PHE B 362
SHEET 8 AA4 8 CYS B 496 GLY B 504 1 O LYS B 497 N LEU B 472
LINK C LEU A 63 N1 CRO A 64 1555 1555 1.43
LINK C3 CRO A 64 N VAL A 67 1555 1555 1.43
LINK OD2 ASP A 340 C20 OEH A 601 1555 1555 1.38
LINK C LEU B 63 N1 CRO B 64 1555 1555 1.43
LINK C3 CRO B 64 N VAL B 67 1555 1555 1.43
LINK OD2 ASP B 340 C20 OEH B 601 1555 1555 1.38
CISPEP 1 MET A 87 PRO A 88 0 6.70
CISPEP 2 ASN A 275 PRO A 276 0 -0.91
CISPEP 3 GLU A 448 PRO A 449 0 -5.23
CISPEP 4 THR A 476 PRO A 477 0 6.31
CISPEP 5 MET B 87 PRO B 88 0 3.55
CISPEP 6 ASN B 275 PRO B 276 0 -0.44
CISPEP 7 GLU B 448 PRO B 449 0 -6.41
CISPEP 8 THR B 476 PRO B 477 0 6.38
CRYST1 46.190 63.710 89.420 93.56 91.02 90.85 P 1 2
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 0.021650 0.000321 0.000404 0.00000
SCALE2 0.000000 0.015698 0.000981 0.00000
SCALE3 0.000000 0.000000 0.011207 0.00000
TER 4160 ILE A 529
TER 8317 ILE B 529
MASTER 280 0 8 47 40 0 0 6 8865 2 150 82
END |