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HEADER HYDROLASE 27-MAY-25 9RBN
TITLE STRUCTURE OF AN ANCESTRAL BIFUNCTIONAL DEHALOGENASE-LUCIFERASE ENZYME
TITLE 2 ANC238LOC, SPACE GROUP C121
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANCESTRAL BIFUNCTIONAL DEHALOGENASE-LUCIFERASE ENZYME
COMPND 3 ANC238LOC;
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 BIFUNCTIONAL DEHALOGENASE-LUCIFERASE ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAREK,M.MAJEROVA
REVDAT 1 27-MAY-26 9RBN 0
JRNL AUTH M.MAJEROVA,J.HORACKOVA,K.SEDLACKOVA,M.SULOVA,D.KOVAR,
JRNL AUTH 2 J.DAMBORSKY,Z.PROKOP,D.BEDNAR,M.MAREK
JRNL TITL STRUCTURAL INSIGHTS INTO THE EVOLUTION OF
JRNL TITL 2 ALPHA/BETA-HYDROLASE FOLD LUCIFERASES.
JRNL REF INT.J.BIOL.MACROMOL. V. 361 51870 2026
JRNL REFN ISSN 0141-8130
JRNL PMID 41951082
JRNL DOI 10.1016/J.IJBIOMAC.2026.151870
REMARK 2
REMARK 2 RESOLUTION. 1.60 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 79214
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) : 0.159
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 3977
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 45.2240 - 4.8520 1.00 2817 123 0.1395 0.1478
REMARK 3 2 4.8520 - 3.8518 0.99 2754 139 0.1166 0.1494
REMARK 3 3 3.8518 - 3.3651 1.00 2727 154 0.1422 0.1937
REMARK 3 4 3.3651 - 3.0575 1.00 2738 137 0.1499 0.1892
REMARK 3 5 3.0575 - 2.8384 1.00 2730 160 0.1649 0.1853
REMARK 3 6 2.8384 - 2.6710 1.00 2704 141 0.1580 0.2095
REMARK 3 7 2.6710 - 2.5373 0.99 2698 136 0.1570 0.1886
REMARK 3 8 2.5373 - 2.4269 0.99 2730 139 0.1554 0.1989
REMARK 3 9 2.4269 - 2.3334 0.99 2690 139 0.1498 0.2004
REMARK 3 10 2.3334 - 2.2529 0.99 2699 165 0.1543 0.2045
REMARK 3 11 2.2529 - 2.1825 0.99 2662 154 0.1589 0.2084
REMARK 3 12 2.1825 - 2.1201 0.99 2709 146 0.1573 0.2053
REMARK 3 13 2.1201 - 2.0643 0.99 2703 133 0.1683 0.2043
REMARK 3 14 2.0643 - 2.0139 0.99 2650 144 0.1717 0.2088
REMARK 3 15 2.0139 - 1.9681 0.99 2704 149 0.1760 0.2130
REMARK 3 16 1.9681 - 1.9262 0.98 2699 146 0.1682 0.2452
REMARK 3 17 1.9262 - 1.8877 0.99 2651 124 0.1752 0.2207
REMARK 3 18 1.8877 - 1.8521 0.99 2708 139 0.1772 0.2265
REMARK 3 19 1.8521 - 1.8190 0.98 2645 142 0.1836 0.2119
REMARK 3 20 1.8190 - 1.7882 0.98 2686 131 0.1925 0.2471
REMARK 3 21 1.7882 - 1.7593 0.98 2634 165 0.2025 0.2757
REMARK 3 22 1.7593 - 1.7323 0.98 2648 139 0.2185 0.2475
REMARK 3 23 1.7323 - 1.7068 0.98 2638 151 0.2256 0.3034
REMARK 3 24 1.7068 - 1.6827 0.98 2658 137 0.2443 0.2695
REMARK 3 25 1.6827 - 1.6600 0.98 2657 133 0.2555 0.2954
REMARK 3 26 1.6600 - 1.6384 0.98 2688 128 0.2756 0.3033
REMARK 3 27 1.6384 - 1.6180 0.97 2624 146 0.2805 0.3365
REMARK 3 28 1.6180 - 1.5985 0.95 2586 137 0.3149 0.3505
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.870
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 : 0.014 5236
REMARK 3 ANGLE : 1.300 7085
REMARK 3 CHIRALITY : 0.081 727
REMARK 3 PLANARITY : 0.009 906
REMARK 3 DIHEDRAL : 5.911 5014
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): 36.6686 -0.5883 22.6640
REMARK 3 T TENSOR
REMARK 3 T11: 0.2386 T22: 0.1629
REMARK 3 T33: 0.1801 T12: -0.0122
REMARK 3 T13: 0.0046 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.8087 L22: 0.2017
REMARK 3 L33: 0.4463 L12: -0.1489
REMARK 3 L13: 0.3516 L23: -0.0354
REMARK 3 S TENSOR
REMARK 3 S11: -0.0063 S12: -0.0237 S13: -0.0030
REMARK 3 S21: -0.0255 S22: 0.0045 S23: 0.0129
REMARK 3 S31: 0.0015 S32: 0.0194 S33: -0.0021
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 9RBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-25.
REMARK 100 THE DEPOSITION ID IS D_1292148140.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-21
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79229
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.598
REMARK 200 RESOLUTION RANGE LOW (A) : 46.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 1.11400
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, MOPS, PEG 500MME, PEG 20000,
REMARK 280 AMINO ACIDS, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293.15K
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 41.75050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.88650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 41.75050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.88650
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 MET A 1
REMARK 465 VAL A 2
REMARK 465 THR A 310
REMARK 465 ASN A 311
REMARK 465 SER A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 SER B 3
REMARK 465 HIS B 4
REMARK 465 PRO B 5
REMARK 465 GLN B 6
REMARK 465 SER B 7
REMARK 465 THR B 8
REMARK 465 ARG B 9
REMARK 465 THR B 310
REMARK 465 ASN B 311
REMARK 465 SER B 312
REMARK 465 HIS B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 HIS B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
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 11 135.15 -35.23
REMARK 500 LEU A 27 -122.82 49.51
REMARK 500 SER A 29 -151.94 -143.92
REMARK 500 GLU A 37 79.47 -154.51
REMARK 500 PRO A 54 46.23 -108.42
REMARK 500 THR A 55 -156.66 -104.22
REMARK 500 PRO A 111 160.52 -45.98
REMARK 500 ASP A 120 -132.71 55.33
REMARK 500 ILE A 159 -42.70 71.89
REMARK 500 LYS A 210 154.06 -47.65
REMARK 500 PHE A 262 -63.48 -126.14
REMARK 500 LEU A 285 -134.52 -102.71
REMARK 500 LEU B 27 -126.86 55.42
REMARK 500 SER B 29 -151.01 -142.30
REMARK 500 HIS B 39 -107.20 -124.02
REMARK 500 PRO B 54 45.50 -109.95
REMARK 500 THR B 55 -155.00 -103.59
REMARK 500 ASP B 120 -133.95 54.03
REMARK 500 GLN B 148 149.65 -170.80
REMARK 500 GLU B 229 -68.39 -120.14
REMARK 500 PHE B 262 -61.11 -126.99
REMARK 500 LEU B 285 -133.13 -101.31
REMARK 500 PHE B 287 56.92 -91.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 769 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH B 770 DISTANCE = 6.51 ANGSTROMS
DBREF 9RBN A 1 318 PDB 9RBN 9RBN 1 318
DBREF 9RBN B 1 318 PDB 9RBN 9RBN 1 318
SEQRES 1 A 318 MET VAL SER HIS PRO GLN SER THR ARG PRO LEU ILE THR
SEQRES 2 A 318 ALA ASP GLU TRP TRP GLY LYS CYS LYS LYS ILE ASN VAL
SEQRES 3 A 318 LEU ASP SER TYR MET SER TYR TYR ASP SER GLU PRO HIS
SEQRES 4 A 318 ASN LEU SER GLY LYS ASN THR VAL VAL PHE LEU HIS GLY
SEQRES 5 A 318 ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO
SEQRES 6 A 318 HIS VAL GLU PRO ILE ALA ARG CYS LEU ALA PRO ASP LEU
SEQRES 7 A 318 ILE GLY MET GLY ARG SER GLY LYS LEU GLY ASN GLY SER
SEQRES 8 A 318 TYR ARG PHE LEU ASP HIS TYR LYS TYR LEU SER ALA TRP
SEQRES 9 A 318 PHE ASP ALA LEU LYS LEU PRO GLU LYS ILE THR ILE VAL
SEQRES 10 A 318 CYS HIS ASP TRP GLY SER GLY LEU GLY PHE HIS TRP CYS
SEQRES 11 A 318 HIS GLU HIS PRO ASP ARG VAL LYS ALA ILE VAL HIS MET
SEQRES 12 A 318 GLU SER VAL VAL GLN PRO ILE ARG SER TRP GLU THR TRP
SEQRES 13 A 318 PRO ASP ILE ALA ARG ASP ILE PHE GLN ALA LEU ARG SER
SEQRES 14 A 318 ASP ALA GLY GLU GLU MET ILE LEU LYS LYS ASN PHE PHE
SEQRES 15 A 318 ILE GLU ARG LEU LEU PRO SER SER ILE MET ARG LYS LEU
SEQRES 16 A 318 ARG PRO GLU GLU MET ASP ALA TYR ARG GLU PRO PHE LYS
SEQRES 17 A 318 GLU LYS GLY GLU SER ARG ARG PRO MET LEU THR TRP PRO
SEQRES 18 A 318 ARG GLU ILE PRO ILE GLU GLY GLU GLY PRO GLU ASP VAL
SEQRES 19 A 318 LEU LYS ILE VAL SER ASP TYR HIS ALA PHE MET LYS ALA
SEQRES 20 A 318 SER GLU ASP LEU PRO LYS LEU PHE ILE GLU ALA ASP PRO
SEQRES 21 A 318 GLY PHE PHE SER LYS ALA ILE THR GLU ILE ALA LYS GLN
SEQRES 22 A 318 TRP PRO ASN THR LYS VAL VAL LYS VAL LYS GLY LEU HIS
SEQRES 23 A 318 PHE LEU GLN GLU ASP SER PRO ASP GLU ILE GLY ASN ALA
SEQRES 24 A 318 ILE LYS GLU PHE LEU GLU LYS VAL PHE LYS THR ASN SER
SEQRES 25 A 318 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 318 MET VAL SER HIS PRO GLN SER THR ARG PRO LEU ILE THR
SEQRES 2 B 318 ALA ASP GLU TRP TRP GLY LYS CYS LYS LYS ILE ASN VAL
SEQRES 3 B 318 LEU ASP SER TYR MET SER TYR TYR ASP SER GLU PRO HIS
SEQRES 4 B 318 ASN LEU SER GLY LYS ASN THR VAL VAL PHE LEU HIS GLY
SEQRES 5 B 318 ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO
SEQRES 6 B 318 HIS VAL GLU PRO ILE ALA ARG CYS LEU ALA PRO ASP LEU
SEQRES 7 B 318 ILE GLY MET GLY ARG SER GLY LYS LEU GLY ASN GLY SER
SEQRES 8 B 318 TYR ARG PHE LEU ASP HIS TYR LYS TYR LEU SER ALA TRP
SEQRES 9 B 318 PHE ASP ALA LEU LYS LEU PRO GLU LYS ILE THR ILE VAL
SEQRES 10 B 318 CYS HIS ASP TRP GLY SER GLY LEU GLY PHE HIS TRP CYS
SEQRES 11 B 318 HIS GLU HIS PRO ASP ARG VAL LYS ALA ILE VAL HIS MET
SEQRES 12 B 318 GLU SER VAL VAL GLN PRO ILE ARG SER TRP GLU THR TRP
SEQRES 13 B 318 PRO ASP ILE ALA ARG ASP ILE PHE GLN ALA LEU ARG SER
SEQRES 14 B 318 ASP ALA GLY GLU GLU MET ILE LEU LYS LYS ASN PHE PHE
SEQRES 15 B 318 ILE GLU ARG LEU LEU PRO SER SER ILE MET ARG LYS LEU
SEQRES 16 B 318 ARG PRO GLU GLU MET ASP ALA TYR ARG GLU PRO PHE LYS
SEQRES 17 B 318 GLU LYS GLY GLU SER ARG ARG PRO MET LEU THR TRP PRO
SEQRES 18 B 318 ARG GLU ILE PRO ILE GLU GLY GLU GLY PRO GLU ASP VAL
SEQRES 19 B 318 LEU LYS ILE VAL SER ASP TYR HIS ALA PHE MET LYS ALA
SEQRES 20 B 318 SER GLU ASP LEU PRO LYS LEU PHE ILE GLU ALA ASP PRO
SEQRES 21 B 318 GLY PHE PHE SER LYS ALA ILE THR GLU ILE ALA LYS GLN
SEQRES 22 B 318 TRP PRO ASN THR LYS VAL VAL LYS VAL LYS GLY LEU HIS
SEQRES 23 B 318 PHE LEU GLN GLU ASP SER PRO ASP GLU ILE GLY ASN ALA
SEQRES 24 B 318 ILE LYS GLU PHE LEU GLU LYS VAL PHE LYS THR ASN SER
SEQRES 25 B 318 HIS HIS HIS HIS HIS HIS
HET PGE A 401 10
HET PGE A 402 10
HET 1PE B 401 16
HET PGE B 402 10
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 PGE 3(C6 H14 O4)
FORMUL 5 1PE C10 H22 O6
FORMUL 7 HOH *560(H2 O)
HELIX 1 AA1 THR A 13 LYS A 20 1 8
HELIX 2 AA2 SER A 56 ARG A 61 5 6
HELIX 3 AA3 ILE A 63 GLU A 68 1 6
HELIX 4 AA4 ARG A 93 LYS A 109 1 17
HELIX 5 AA5 ASP A 120 HIS A 133 1 14
HELIX 6 AA6 SER A 152 TRP A 156 5 5
HELIX 7 AA7 ILE A 159 SER A 169 1 11
HELIX 8 AA8 ALA A 171 LYS A 178 1 8
HELIX 9 AA9 ASN A 180 ARG A 185 1 6
HELIX 10 AB1 ARG A 185 SER A 190 1 6
HELIX 11 AB2 ARG A 196 GLU A 205 1 10
HELIX 12 AB3 PRO A 206 LYS A 208 5 3
HELIX 13 AB4 GLY A 211 SER A 213 5 3
HELIX 14 AB5 ARG A 214 GLU A 223 1 10
HELIX 15 AB6 PRO A 231 SER A 248 1 18
HELIX 16 AB7 PHE A 263 TRP A 274 1 12
HELIX 17 AB8 PHE A 287 ASP A 291 5 5
HELIX 18 AB9 SER A 292 LYS A 309 1 18
HELIX 19 AC1 THR B 13 LYS B 20 1 8
HELIX 20 AC2 SER B 56 ARG B 61 5 6
HELIX 21 AC3 ILE B 63 GLU B 68 1 6
HELIX 22 AC4 ARG B 93 LEU B 108 1 16
HELIX 23 AC5 ASP B 120 HIS B 133 1 14
HELIX 24 AC6 SER B 152 TRP B 156 5 5
HELIX 25 AC7 PRO B 157 SER B 169 1 13
HELIX 26 AC8 ASP B 170 LYS B 178 1 9
HELIX 27 AC9 ASN B 180 ARG B 185 1 6
HELIX 28 AD1 ARG B 185 SER B 190 1 6
HELIX 29 AD2 ARG B 196 GLU B 205 1 10
HELIX 30 AD3 PRO B 206 LYS B 208 5 3
HELIX 31 AD4 GLY B 211 SER B 213 5 3
HELIX 32 AD5 ARG B 214 GLU B 223 1 10
HELIX 33 AD6 PRO B 231 SER B 248 1 18
HELIX 34 AD7 PHE B 263 GLN B 273 1 11
HELIX 35 AD8 PHE B 287 ASP B 291 5 5
HELIX 36 AD9 SER B 292 LYS B 309 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 ALA A 71 PRO A 76 -1 O ALA A 75 N TYR A 34
SHEET 4 AA1 8 ASN A 45 LEU A 50 1 N PHE A 49 O LEU A 74
SHEET 5 AA1 8 ILE A 114 HIS A 119 1 O THR A 115 N VAL A 48
SHEET 6 AA1 8 VAL A 137 MET A 143 1 O VAL A 141 N ILE A 116
SHEET 7 AA1 8 LYS A 253 PRO A 260 1 O LEU A 254 N HIS A 142
SHEET 8 AA1 8 THR A 277 GLY A 284 1 O LYS A 278 N PHE A 255
SHEET 1 AA2 8 CYS B 21 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 ALA B 71 PRO B 76 -1 O ALA B 75 N TYR B 34
SHEET 4 AA2 8 ASN B 45 LEU B 50 1 N VAL B 47 O ARG B 72
SHEET 5 AA2 8 ILE B 114 HIS B 119 1 O THR B 115 N VAL B 48
SHEET 6 AA2 8 VAL B 137 MET B 143 1 O LYS B 138 N ILE B 114
SHEET 7 AA2 8 LYS B 253 PRO B 260 1 O LEU B 254 N HIS B 142
SHEET 8 AA2 8 THR B 277 GLY B 284 1 O LYS B 278 N PHE B 255
CISPEP 1 ASN A 53 PRO A 54 0 4.12
CISPEP 2 GLY A 230 PRO A 231 0 -0.50
CISPEP 3 ASP A 259 PRO A 260 0 7.58
CISPEP 4 ASN B 53 PRO B 54 0 4.12
CISPEP 5 GLY B 230 PRO B 231 0 2.66
CISPEP 6 ASP B 259 PRO B 260 0 2.31
CRYST1 83.501 81.773 91.726 90.00 99.57 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 0.011976 0.000000 0.002020 0.00000
SCALE2 0.000000 0.012229 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011056 0.00000
TER 2561 LYS A 309
TER 5034 LYS B 309
MASTER 327 0 4 36 16 0 0 6 5564 2 46 50
END |