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HEADER LUMINESCENT PROTEIN 03-JUL-19 6S6E
TITLE CRYSTAL STRUCTURE OF THE ENGINEERED ANCESTOR OF HALOALKANE
TITLE 2 DEHALOGENASES AND RENILLA LUCIFERASE (ANCHLD-RLUC I161_F162PINSL)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENGINEERED ANCESTOR OF HALOALKANE DEHALOGENASES AND RENILLA
COMPND 3 LUCIFERASE (ANCHLD-RLUC I161_F162PINSL);
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENGINEERED ANCESTRAL ENZYME, BIOLUMINSCENCE, COELENTERAZINE-UTILIZING
KEYWDS 2 ENZYME, LUMINESCENT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHENKMAYEROVA,J.DAMBORSKY,M.MAREK
REVDAT 1 27-JAN-21 6S6E 0
JRNL AUTH A.SCHENKMAYEROVA,M.MAREK,J.DAMBORSKY
JRNL TITL INSERTION-DELETION MUTAGENESIS OF A THERMOSTABLE ANCESTRAL
JRNL TITL 2 ENZYME CONFERS PROTEIN BACKBONE MOTIONS BEING ESSENTIAL FOR
JRNL TITL 3 THE EMERGENCE OF ENZYMATIC FUNCTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 41591
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 2051
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 45.0940 - 4.9332 0.99 2850 135 0.1541 0.1758
REMARK 3 2 4.9332 - 3.9164 1.00 2716 153 0.1294 0.1448
REMARK 3 3 3.9164 - 3.4215 1.00 2634 143 0.1606 0.2035
REMARK 3 4 3.4215 - 3.1088 1.00 2683 129 0.1804 0.2644
REMARK 3 5 3.1088 - 2.8860 1.00 2622 152 0.1992 0.2392
REMARK 3 6 2.8860 - 2.7159 1.00 2641 128 0.1894 0.2335
REMARK 3 7 2.7159 - 2.5799 1.00 2631 142 0.2010 0.2686
REMARK 3 8 2.5799 - 2.4676 1.00 2597 149 0.1806 0.2030
REMARK 3 9 2.4676 - 2.3726 1.00 2613 126 0.1765 0.2572
REMARK 3 10 2.3726 - 2.2907 1.00 2622 126 0.1771 0.2413
REMARK 3 11 2.2907 - 2.2191 1.00 2593 126 0.1786 0.2855
REMARK 3 12 2.2191 - 2.1557 1.00 2605 139 0.1887 0.2679
REMARK 3 13 2.1557 - 2.0989 1.00 2605 143 0.2060 0.2775
REMARK 3 14 2.0989 - 2.0477 1.00 2574 138 0.2167 0.2966
REMARK 3 15 2.0477 - 2.0011 0.98 2554 122 0.2057 0.2324
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.25
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 : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8971 8.9763 -46.4378
REMARK 3 T TENSOR
REMARK 3 T11: 0.2251 T22: 0.1934
REMARK 3 T33: 0.2612 T12: -0.0211
REMARK 3 T13: -0.0031 T23: 0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 0.2571 L22: 0.3634
REMARK 3 L33: 3.1895 L12: 0.1042
REMARK 3 L13: 0.1828 L23: 0.7786
REMARK 3 S TENSOR
REMARK 3 S11: -0.0620 S12: 0.0280 S13: 0.0301
REMARK 3 S21: -0.1949 S22: 0.0037 S23: 0.0235
REMARK 3 S31: -0.3726 S32: 0.0536 S33: 0.0180
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 6S6E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1292103190.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.86099
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.6.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41733
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 45.094
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : 0.70700
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.0
REMARK 200 STARTING MODEL: 6G75
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 500MME, PEG 20000, SODIUM NITRATE,
REMARK 280 SODIUM PHOSPHATE DIBASIC, AMMONIUM SULPHATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
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 22.35700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.10750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.08450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.10750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.35700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.08450
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 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 LYS A 308
REMARK 465 THR B 11
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 ALA A 12 87.18 69.43
REMARK 500 LEU A 27 -129.84 48.43
REMARK 500 SER A 29 -159.15 -145.55
REMARK 500 ASP A 37 72.99 -153.59
REMARK 500 PRO A 52 44.39 -106.86
REMARK 500 THR A 53 -155.51 -99.06
REMARK 500 HIS A 88 41.76 36.72
REMARK 500 ASP A 118 -129.65 59.12
REMARK 500 PRO A 163 -71.60 -75.18
REMARK 500 GLN A 164 155.27 -48.48
REMARK 500 ALA A 165 -100.20 72.71
REMARK 500 ASP A 228 -74.76 -80.71
REMARK 500 PHE A 261 -70.86 -130.53
REMARK 500 LEU A 284 -132.80 -99.06
REMARK 500 LEU B 27 -123.29 48.90
REMARK 500 SER B 29 -150.08 -147.20
REMARK 500 ASP B 37 86.41 -159.99
REMARK 500 LYS B 42 -166.72 -73.56
REMARK 500 THR B 53 -153.46 -100.19
REMARK 500 ASN B 107 71.57 66.01
REMARK 500 ASP B 118 -132.14 56.68
REMARK 500 ASP B 228 -61.59 -95.79
REMARK 500 PHE B 261 -74.28 -125.32
REMARK 500 LEU B 284 -136.44 -95.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 159 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6S6E A 11 308 PDB 6S6E 6S6E 11 308
DBREF 6S6E B 11 308 PDB 6S6E 6S6E 11 308
SEQRES 1 A 298 THR ALA THR GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN
SEQRES 2 A 298 VAL ASP VAL LEU ASP SER GLU MET SER TYR TYR ASP SER
SEQRES 3 A 298 ASP PRO GLY LYS HIS LYS ASN THR VAL ILE PHE LEU HIS
SEQRES 4 A 298 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE
SEQRES 5 A 298 PRO HIS VAL GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP
SEQRES 6 A 298 LEU ILE GLY MET GLY LYS SER GLY LYS LEU PRO ASN HIS
SEQRES 7 A 298 SER TYR ARG PHE VAL ASP HIS TYR ARG TYR LEU SER ALA
SEQRES 8 A 298 TRP PHE ASP SER VAL ASN LEU PRO GLU LYS VAL THR ILE
SEQRES 9 A 298 VAL CYS HIS ASP TRP GLY SER GLY LEU GLY PHE HIS TRP
SEQRES 10 A 298 CYS ASN GLU HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS
SEQRES 11 A 298 MET GLU SER VAL VAL SER PRO LEU LYS GLY TRP GLU SER
SEQRES 12 A 298 PHE PRO GLU THR ALA ARG ASP ILE LEU PRO GLN ALA LEU
SEQRES 13 A 298 ARG SER GLU ALA GLY GLU GLU MET VAL LEU LYS LYS ASN
SEQRES 14 A 298 PHE PHE ILE GLU ARG LEU LEU PRO SER SER ILE MET ARG
SEQRES 15 A 298 LYS LEU SER GLU GLU GLU MET ASP ALA TYR ARG GLU PRO
SEQRES 16 A 298 PHE VAL GLU PRO GLY GLU SER ARG ARG PRO THR LEU THR
SEQRES 17 A 298 TRP PRO ARG GLU ILE PRO ILE LYS GLY ASP GLY PRO GLU
SEQRES 18 A 298 ASP VAL ILE GLU ILE VAL LYS SER TYR ASN LYS TRP LEU
SEQRES 19 A 298 SER THR SER LYS ASP ILE PRO LYS LEU PHE ILE ASN ALA
SEQRES 20 A 298 ASP PRO GLY PHE PHE SER ASN ALA ILE LYS LYS VAL THR
SEQRES 21 A 298 LYS ASN TRP PRO ASN GLN LYS THR VAL THR VAL LYS GLY
SEQRES 22 A 298 LEU HIS PHE LEU GLN GLU ASP SER PRO GLU GLU ILE GLY
SEQRES 23 A 298 GLU ALA ILE ALA ASP PHE LEU ASN GLU LEU THR LYS
SEQRES 1 B 298 THR ALA THR GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN
SEQRES 2 B 298 VAL ASP VAL LEU ASP SER GLU MET SER TYR TYR ASP SER
SEQRES 3 B 298 ASP PRO GLY LYS HIS LYS ASN THR VAL ILE PHE LEU HIS
SEQRES 4 B 298 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE
SEQRES 5 B 298 PRO HIS VAL GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP
SEQRES 6 B 298 LEU ILE GLY MET GLY LYS SER GLY LYS LEU PRO ASN HIS
SEQRES 7 B 298 SER TYR ARG PHE VAL ASP HIS TYR ARG TYR LEU SER ALA
SEQRES 8 B 298 TRP PHE ASP SER VAL ASN LEU PRO GLU LYS VAL THR ILE
SEQRES 9 B 298 VAL CYS HIS ASP TRP GLY SER GLY LEU GLY PHE HIS TRP
SEQRES 10 B 298 CYS ASN GLU HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS
SEQRES 11 B 298 MET GLU SER VAL VAL SER PRO LEU LYS GLY TRP GLU SER
SEQRES 12 B 298 PHE PRO GLU THR ALA ARG ASP ILE LEU PRO GLN ALA LEU
SEQRES 13 B 298 ARG SER GLU ALA GLY GLU GLU MET VAL LEU LYS LYS ASN
SEQRES 14 B 298 PHE PHE ILE GLU ARG LEU LEU PRO SER SER ILE MET ARG
SEQRES 15 B 298 LYS LEU SER GLU GLU GLU MET ASP ALA TYR ARG GLU PRO
SEQRES 16 B 298 PHE VAL GLU PRO GLY GLU SER ARG ARG PRO THR LEU THR
SEQRES 17 B 298 TRP PRO ARG GLU ILE PRO ILE LYS GLY ASP GLY PRO GLU
SEQRES 18 B 298 ASP VAL ILE GLU ILE VAL LYS SER TYR ASN LYS TRP LEU
SEQRES 19 B 298 SER THR SER LYS ASP ILE PRO LYS LEU PHE ILE ASN ALA
SEQRES 20 B 298 ASP PRO GLY PHE PHE SER ASN ALA ILE LYS LYS VAL THR
SEQRES 21 B 298 LYS ASN TRP PRO ASN GLN LYS THR VAL THR VAL LYS GLY
SEQRES 22 B 298 LEU HIS PHE LEU GLN GLU ASP SER PRO GLU GLU ILE GLY
SEQRES 23 B 298 GLU ALA ILE ALA ASP PHE LEU ASN GLU LEU THR LYS
FORMUL 3 HOH *175(H2 O)
HELIX 1 AA1 THR A 13 LYS A 20 1 8
HELIX 2 AA2 SER A 54 ARG A 59 5 6
HELIX 3 AA3 VAL A 61 VAL A 65 5 5
HELIX 4 AA4 ARG A 91 ASP A 104 1 14
HELIX 5 AA5 ASP A 118 HIS A 131 1 14
HELIX 6 AA6 GLY A 150 PHE A 154 5 5
HELIX 7 AA7 PRO A 155 ARG A 159 5 5
HELIX 8 AA8 GLN A 164 GLU A 169 5 6
HELIX 9 AA9 ALA A 170 LYS A 177 1 8
HELIX 10 AB1 ASN A 179 ARG A 184 1 6
HELIX 11 AB2 ARG A 184 SER A 189 1 6
HELIX 12 AB3 SER A 195 GLU A 204 1 10
HELIX 13 AB4 PRO A 205 VAL A 207 5 3
HELIX 14 AB5 GLY A 210 SER A 212 5 3
HELIX 15 AB6 ARG A 213 GLU A 222 1 10
HELIX 16 AB7 PRO A 230 THR A 246 1 17
HELIX 17 AB8 PHE A 262 THR A 270 1 9
HELIX 18 AB9 PHE A 286 ASP A 290 5 5
HELIX 19 AC1 SER A 291 THR A 307 1 17
HELIX 20 AC2 THR B 13 ALA B 19 1 7
HELIX 21 AC3 SER B 54 ARG B 59 5 6
HELIX 22 AC4 VAL B 61 ALA B 69 5 9
HELIX 23 AC5 ARG B 91 ASP B 104 1 14
HELIX 24 AC6 ASP B 118 HIS B 131 1 14
HELIX 25 AC7 GLY B 150 PHE B 154 5 5
HELIX 26 AC8 PRO B 155 GLU B 156 5 2
HELIX 27 AC9 THR B 157 LEU B 162 1 6
HELIX 28 AD1 PRO B 163 GLU B 169 5 7
HELIX 29 AD2 ALA B 170 LYS B 177 1 8
HELIX 30 AD3 ASN B 179 ARG B 184 1 6
HELIX 31 AD4 ARG B 184 SER B 189 1 6
HELIX 32 AD5 SER B 195 GLU B 204 1 10
HELIX 33 AD6 PRO B 205 VAL B 207 5 3
HELIX 34 AD7 GLY B 210 SER B 212 5 3
HELIX 35 AD8 ARG B 213 GLU B 222 1 10
HELIX 36 AD9 PRO B 230 SER B 245 1 16
HELIX 37 AE1 PHE B 262 THR B 270 1 9
HELIX 38 AE2 PHE B 286 ASP B 290 5 5
HELIX 39 AE3 SER B 291 LYS B 308 1 18
SHEET 1 AA1 8 LYS A 22 VAL A 26 0
SHEET 2 AA1 8 SER A 29 ASP A 35 -1 O SER A 29 N VAL A 26
SHEET 3 AA1 8 ARG A 70 PRO A 74 -1 O ALA A 73 N TYR A 34
SHEET 4 AA1 8 THR A 44 LEU A 48 1 N VAL A 45 O ARG A 70
SHEET 5 AA1 8 VAL A 112 HIS A 117 1 O VAL A 115 N ILE A 46
SHEET 6 AA1 8 VAL A 135 MET A 141 1 O VAL A 139 N ILE A 114
SHEET 7 AA1 8 LYS A 252 PRO A 259 1 O ILE A 255 N HIS A 140
SHEET 8 AA1 8 GLN A 276 GLY A 283 1 O LYS A 277 N PHE A 254
SHEET 1 AA2 8 LYS B 22 VAL B 26 0
SHEET 2 AA2 8 SER B 29 ASP B 35 -1 O SER B 29 N VAL B 26
SHEET 3 AA2 8 ARG B 70 PRO B 74 -1 O ALA B 73 N TYR B 34
SHEET 4 AA2 8 THR B 44 LEU B 48 1 N PHE B 47 O LEU B 72
SHEET 5 AA2 8 VAL B 112 HIS B 117 1 O VAL B 115 N ILE B 46
SHEET 6 AA2 8 VAL B 135 MET B 141 1 O LYS B 136 N VAL B 112
SHEET 7 AA2 8 LYS B 252 PRO B 259 1 O LEU B 253 N ILE B 138
SHEET 8 AA2 8 GLN B 276 GLY B 283 1 O VAL B 281 N ASP B 258
CISPEP 1 ASN A 51 PRO A 52 0 0.33
CISPEP 2 GLY A 229 PRO A 230 0 -1.36
CISPEP 3 ASP A 258 PRO A 259 0 6.00
CISPEP 4 ASN B 51 PRO B 52 0 -0.68
CISPEP 5 GLY B 229 PRO B 230 0 -3.76
CISPEP 6 ASP B 258 PRO B 259 0 3.07
CRYST1 44.714 84.169 160.215 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 0.022364 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011881 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006242 0.00000
TER 2403 THR A 307
TER 4817 LYS B 308
MASTER 290 0 0 39 16 0 0 6 4981 2 0 46
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