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HEADER HYDROLASE 04-APR-18 6G75
TITLE CRYSTAL STRUCTURE OF THE COMMON ANCESTOR OF HALOALKANE DEHALOGENASES
TITLE 2 AND RENILLA LUCIFERASE (ANCHLD-RLUC)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMMON ANCESTOR OF HALOALKANE DEHALOGENASE AND RENILLA
COMPND 3 LUCIFERASE (ANCHLD-RLUC);
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 BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS HALOALKANE DEHALOGENASE, RENILLA LUCIFERASE, OXYGEN-BOUND, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CHALOUPKOVA,J.WATERMAN,M.MAREK,J.DAMBORSKY
REVDAT 1 24-APR-19 6G75 0
JRNL AUTH R.CHALOUPKOVA,V.LISKOVA
JRNL TITL CRYSTAL STRUCTURE OF THE COMMON ANCESTOR OF HALOALKANE
JRNL TITL 2 DEHALOGENASES AND RENILLA LUCIFERASE (ANCHLD-RLUC)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.39 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 122118
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 6022
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 21.6218 - 4.3111 0.96 4121 225 0.1483 0.1539
REMARK 3 2 4.3111 - 3.4263 0.96 4025 220 0.1347 0.1645
REMARK 3 3 3.4263 - 2.9944 0.94 4011 176 0.1503 0.1820
REMARK 3 4 2.9944 - 2.7212 0.96 4049 220 0.1592 0.2108
REMARK 3 5 2.7212 - 2.5265 0.96 4013 190 0.1516 0.1824
REMARK 3 6 2.5265 - 2.3777 0.96 4012 209 0.1484 0.1829
REMARK 3 7 2.3777 - 2.2588 0.95 3984 216 0.1417 0.1768
REMARK 3 8 2.2588 - 2.1606 0.94 3945 167 0.1397 0.1788
REMARK 3 9 2.1606 - 2.0775 0.94 3885 248 0.1359 0.1715
REMARK 3 10 2.0775 - 2.0058 0.93 3917 197 0.1365 0.1889
REMARK 3 11 2.0058 - 1.9431 0.93 3867 176 0.1304 0.1588
REMARK 3 12 1.9431 - 1.8876 0.92 3871 185 0.1282 0.1751
REMARK 3 13 1.8876 - 1.8380 0.91 3787 196 0.1328 0.1778
REMARK 3 14 1.8380 - 1.7931 0.92 3806 190 0.1335 0.1774
REMARK 3 15 1.7931 - 1.7524 0.91 3841 195 0.1315 0.1970
REMARK 3 16 1.7524 - 1.7151 0.93 3838 170 0.1299 0.1992
REMARK 3 17 1.7151 - 1.6808 0.91 3880 159 0.1367 0.1817
REMARK 3 18 1.6808 - 1.6491 0.93 3844 211 0.1396 0.1971
REMARK 3 19 1.6491 - 1.6197 0.92 3860 206 0.1430 0.2116
REMARK 3 20 1.6197 - 1.5922 0.93 3779 212 0.1448 0.2203
REMARK 3 21 1.5922 - 1.5666 0.90 3769 224 0.1459 0.1849
REMARK 3 22 1.5666 - 1.5425 0.91 3705 242 0.1661 0.2269
REMARK 3 23 1.5425 - 1.5198 0.90 3764 220 0.1806 0.2369
REMARK 3 24 1.5198 - 1.4984 0.91 3751 213 0.1915 0.2734
REMARK 3 25 1.4984 - 1.4781 0.91 3810 186 0.1973 0.2511
REMARK 3 26 1.4781 - 1.4589 0.91 3849 174 0.2081 0.2469
REMARK 3 27 1.4589 - 1.4407 0.93 3780 196 0.2161 0.2653
REMARK 3 28 1.4407 - 1.4234 0.91 3803 202 0.2275 0.2760
REMARK 3 29 1.4234 - 1.4068 0.91 3775 217 0.2453 0.3030
REMARK 3 30 1.4068 - 1.3910 0.91 3755 180 0.2499 0.3012
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.61
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 : 0.005 5053
REMARK 3 ANGLE : 0.821 6871
REMARK 3 CHIRALITY : 0.083 717
REMARK 3 PLANARITY : 0.006 883
REMARK 3 DIHEDRAL : 2.595 3072
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 6G75 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009489.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-14
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 : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 122192
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
REMARK 200 RESOLUTION RANGE LOW (A) : 21.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.72700
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
REMARK 200 STARTING MODEL: 2PSF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0 AND 10% (W/V) PEG
REMARK 280 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 30.25500
REMARK 290 SMTRY3 2 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 PHE B 180 N CA C O CB CG CD1
REMARK 480 PHE B 180 CD2 CE1 CE2 CZ
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 A 27 -119.55 48.59
REMARK 500 SER A 29 -153.14 -149.50
REMARK 500 ASP A 37 74.24 -158.09
REMARK 500 PRO A 52 48.74 -107.75
REMARK 500 THR A 53 -156.30 -100.95
REMARK 500 ASP A 118 -131.97 54.99
REMARK 500 HIS A 131 57.02 -140.14
REMARK 500 PHE A 260 -65.10 -124.98
REMARK 500 LEU A 283 -137.29 -96.48
REMARK 500 LEU B 27 -122.01 47.86
REMARK 500 SER B 29 -148.09 -149.13
REMARK 500 ASP B 37 74.79 -154.15
REMARK 500 PRO B 52 47.50 -107.95
REMARK 500 THR B 53 -158.23 -101.59
REMARK 500 ASP B 118 -133.01 54.34
REMARK 500 ASP B 227 -53.87 -122.83
REMARK 500 PHE B 260 -67.66 -121.84
REMARK 500 LEU B 283 -136.49 -100.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 403
DBREF 6G75 A 12 307 PDB 6G75 6G75 12 307
DBREF 6G75 B 12 307 PDB 6G75 6G75 12 307
SEQRES 1 A 296 ALA THR GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN VAL
SEQRES 2 A 296 ASP VAL LEU ASP SER GLU MET SER TYR TYR ASP SER ASP
SEQRES 3 A 296 PRO GLY LYS HIS LYS ASN THR VAL ILE PHE LEU HIS GLY
SEQRES 4 A 296 ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE PRO
SEQRES 5 A 296 HIS VAL GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP LEU
SEQRES 6 A 296 ILE GLY MET GLY LYS SER GLY LYS LEU PRO ASN HIS SER
SEQRES 7 A 296 TYR ARG PHE VAL ASP HIS TYR ARG TYR LEU SER ALA TRP
SEQRES 8 A 296 PHE ASP SER VAL ASN LEU PRO GLU LYS VAL THR ILE VAL
SEQRES 9 A 296 CYS HIS ASP TRP GLY SER GLY LEU GLY PHE HIS TRP CYS
SEQRES 10 A 296 ASN GLU HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS MET
SEQRES 11 A 296 GLU SER VAL VAL SER PRO LEU LYS GLY TRP GLU SER PHE
SEQRES 12 A 296 PRO GLU THR ALA ARG ASP ILE PHE GLN ALA LEU ARG SER
SEQRES 13 A 296 GLU ALA GLY GLU GLU MET VAL LEU LYS LYS ASN PHE PHE
SEQRES 14 A 296 ILE GLU ARG LEU LEU PRO SER SER ILE MET ARG LYS LEU
SEQRES 15 A 296 SER GLU GLU GLU MET ASP ALA TYR ARG GLU PRO PHE VAL
SEQRES 16 A 296 GLU PRO GLY GLU SER ARG ARG PRO THR LEU THR TRP PRO
SEQRES 17 A 296 ARG GLU ILE PRO ILE LYS GLY ASP GLY PRO GLU ASP VAL
SEQRES 18 A 296 ILE GLU ILE VAL LYS SER TYR ASN LYS TRP LEU SER THR
SEQRES 19 A 296 SER LYS ASP ILE PRO LYS LEU PHE ILE ASN ALA ASP PRO
SEQRES 20 A 296 GLY PHE PHE SER ASN ALA ILE LYS LYS VAL THR LYS ASN
SEQRES 21 A 296 TRP PRO ASN GLN LYS THR VAL THR VAL LYS GLY LEU HIS
SEQRES 22 A 296 PHE LEU GLN GLU ASP SER PRO GLU GLU ILE GLY GLU ALA
SEQRES 23 A 296 ILE ALA ASP PHE LEU ASN GLU LEU THR LYS
SEQRES 1 B 296 ALA THR GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN VAL
SEQRES 2 B 296 ASP VAL LEU ASP SER GLU MET SER TYR TYR ASP SER ASP
SEQRES 3 B 296 PRO GLY LYS HIS LYS ASN THR VAL ILE PHE LEU HIS GLY
SEQRES 4 B 296 ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE PRO
SEQRES 5 B 296 HIS VAL GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP LEU
SEQRES 6 B 296 ILE GLY MET GLY LYS SER GLY LYS LEU PRO ASN HIS SER
SEQRES 7 B 296 TYR ARG PHE VAL ASP HIS TYR ARG TYR LEU SER ALA TRP
SEQRES 8 B 296 PHE ASP SER VAL ASN LEU PRO GLU LYS VAL THR ILE VAL
SEQRES 9 B 296 CYS HIS ASP TRP GLY SER GLY LEU GLY PHE HIS TRP CYS
SEQRES 10 B 296 ASN GLU HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS MET
SEQRES 11 B 296 GLU SER VAL VAL SER PRO LEU LYS GLY TRP GLU SER PHE
SEQRES 12 B 296 PRO GLU THR ALA ARG ASP ILE PHE GLN ALA LEU ARG SER
SEQRES 13 B 296 GLU ALA GLY GLU GLU MET VAL LEU LYS LYS ASN PHE PHE
SEQRES 14 B 296 ILE GLU ARG LEU LEU PRO SER SER ILE MET ARG LYS LEU
SEQRES 15 B 296 SER GLU GLU GLU MET ASP ALA TYR ARG GLU PRO PHE VAL
SEQRES 16 B 296 GLU PRO GLY GLU SER ARG ARG PRO THR LEU THR TRP PRO
SEQRES 17 B 296 ARG GLU ILE PRO ILE LYS GLY ASP GLY PRO GLU ASP VAL
SEQRES 18 B 296 ILE GLU ILE VAL LYS SER TYR ASN LYS TRP LEU SER THR
SEQRES 19 B 296 SER LYS ASP ILE PRO LYS LEU PHE ILE ASN ALA ASP PRO
SEQRES 20 B 296 GLY PHE PHE SER ASN ALA ILE LYS LYS VAL THR LYS ASN
SEQRES 21 B 296 TRP PRO ASN GLN LYS THR VAL THR VAL LYS GLY LEU HIS
SEQRES 22 B 296 PHE LEU GLN GLU ASP SER PRO GLU GLU ILE GLY GLU ALA
SEQRES 23 B 296 ILE ALA ASP PHE LEU ASN GLU LEU THR LYS
HET OXY A 401 2
HET MPD A 402 8
HET TRS A 403 8
HET OXY B 401 2
HET MPD B 402 8
HET TRS B 403 8
HETNAM OXY OXYGEN MOLECULE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 3 OXY 2(O2)
FORMUL 4 MPD 2(C6 H14 O2)
FORMUL 5 TRS 2(C4 H12 N O3 1+)
FORMUL 9 HOH *465(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 ALA A 69 5 9
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 SER A 167 1 13
HELIX 8 AA8 ALA A 169 LEU A 175 1 7
HELIX 9 AA9 ASN A 178 ARG A 183 1 6
HELIX 10 AB1 ARG A 183 SER A 188 1 6
HELIX 11 AB2 SER A 194 GLU A 203 1 10
HELIX 12 AB3 PRO A 204 VAL A 206 5 3
HELIX 13 AB4 GLY A 209 SER A 211 5 3
HELIX 14 AB5 ARG A 212 ILE A 222 1 11
HELIX 15 AB6 PRO A 229 THR A 245 1 17
HELIX 16 AB7 PHE A 261 THR A 269 1 9
HELIX 17 AB8 PHE A 285 ASP A 289 5 5
HELIX 18 AB9 SER A 290 LYS A 307 1 18
HELIX 19 AC1 THR B 13 LYS B 20 1 8
HELIX 20 AC2 SER B 54 ARG B 59 5 6
HELIX 21 AC3 VAL B 61 ALA B 69 5 9
HELIX 22 AC4 ARG B 91 ASP B 104 1 14
HELIX 23 AC5 ASP B 118 HIS B 131 1 14
HELIX 24 AC6 GLY B 150 PHE B 154 5 5
HELIX 25 AC7 PRO B 155 SER B 167 1 13
HELIX 26 AC8 ALA B 169 LYS B 176 1 8
HELIX 27 AC9 ASN B 178 ARG B 183 1 6
HELIX 28 AD1 ARG B 183 SER B 188 1 6
HELIX 29 AD2 SER B 194 GLU B 203 1 10
HELIX 30 AD3 PRO B 204 VAL B 206 5 3
HELIX 31 AD4 GLY B 209 SER B 211 5 3
HELIX 32 AD5 ARG B 212 ILE B 222 1 11
HELIX 33 AD6 PRO B 229 THR B 245 1 17
HELIX 34 AD7 PHE B 261 THR B 269 1 9
HELIX 35 AD8 PHE B 285 ASP B 289 5 5
HELIX 36 AD9 SER B 290 LYS B 307 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 TYR A 33 N LYS A 22
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 PHE A 47 O LEU A 72
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 251 PRO A 258 1 O LEU A 252 N HIS A 140
SHEET 8 AA1 8 GLN A 275 GLY A 282 1 O LYS A 276 N PHE A 253
SHEET 1 AA2 8 LYS B 22 VAL B 26 0
SHEET 2 AA2 8 SER B 29 ASP B 35 -1 O TYR B 33 N LYS B 22
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 VAL B 45 O ARG B 70
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 VAL B 139 N ILE B 114
SHEET 7 AA2 8 LYS B 251 PRO B 258 1 O ILE B 254 N HIS B 140
SHEET 8 AA2 8 GLN B 275 GLY B 282 1 O VAL B 278 N ASN B 255
CISPEP 1 ASN A 51 PRO A 52 0 -2.63
CISPEP 2 GLY A 228 PRO A 229 0 -1.21
CISPEP 3 ASP A 257 PRO A 258 0 6.10
CISPEP 4 ASN B 51 PRO B 52 0 -1.85
CISPEP 5 GLY B 228 PRO B 229 0 -1.43
CISPEP 6 ASP B 257 PRO B 258 0 3.54
SITE 1 AC1 5 ASN A 51 TRP A 119 PHE A 180 PRO A 219
SITE 2 AC1 5 HOH A 507
SITE 1 AC2 7 PHE A 162 LEU A 184 SER A 188 PHE A 260
SITE 2 AC2 7 HIS A 284 PHE A 285 HOH A 507
SITE 1 AC3 7 SER A 143 VAL A 144 VAL A 145 SER A 146
SITE 2 AC3 7 LEU A 148 PHE A 261 VAL A 268
SITE 1 AC4 5 ASN B 51 TRP B 119 PHE B 180 PRO B 219
SITE 2 AC4 5 HOH B 544
SITE 1 AC5 8 ASP B 118 PHE B 162 PHE B 180 LEU B 184
SITE 2 AC5 8 SER B 188 PHE B 260 HIS B 284 HOH B 544
SITE 1 AC6 6 SER B 143 VAL B 144 VAL B 145 SER B 146
SITE 2 AC6 6 LEU B 148 PHE B 261
CRYST1 44.549 60.510 123.630 90.00 90.90 90.00 P 1 21 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 0.022447 0.000000 0.000353 0.00000
SCALE2 0.000000 0.016526 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008090 0.00000
TER 2438 LYS A 307
TER 4869 LYS B 307
MASTER 284 0 6 36 16 0 12 6 5301 2 36 46
END |