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HEADER HYDROLASE 27-MAY-25 9RBP
TITLE STRUCTURE OF AN ANCESTRAL BIFUNCTIONAL DEHALOGENASE-LUCIFERASE ENZYME
TITLE 2 ANC238LOC, SPACE GROUP P21212
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 9RBP 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. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 31143
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790
REMARK 3 FREE R VALUE TEST SET COUNT : 1493
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 46.8440 - 4.8890 1.00 2896 117 0.1969 0.2714
REMARK 3 2 4.8890 - 3.8811 1.00 2737 156 0.1889 0.2243
REMARK 3 3 3.8811 - 3.3907 1.00 2689 158 0.2052 0.2575
REMARK 3 4 3.3907 - 3.0808 1.00 2690 149 0.2353 0.2880
REMARK 3 5 3.0808 - 2.8600 1.00 2700 127 0.2567 0.3358
REMARK 3 6 2.8600 - 2.6914 1.00 2662 134 0.2726 0.3229
REMARK 3 7 2.6914 - 2.5566 1.00 2680 126 0.2752 0.3492
REMARK 3 8 2.5566 - 2.4453 1.00 2659 125 0.3047 0.3957
REMARK 3 9 2.4453 - 2.3512 1.00 2661 131 0.3213 0.3961
REMARK 3 10 2.3512 - 2.2701 1.00 2661 121 0.3477 0.3981
REMARK 3 11 2.2701 - 2.1991 0.99 2615 149 0.3762 0.4237
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.700
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 : 0.005 4993
REMARK 3 ANGLE : 0.767 6747
REMARK 3 CHIRALITY : 0.046 698
REMARK 3 PLANARITY : 0.005 859
REMARK 3 DIHEDRAL : 7.743 3590
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 9RBP 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_1292148143.
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) : 1.0
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 : 31216
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.199
REMARK 200 RESOLUTION RANGE LOW (A) : 48.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : 0.20700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 12.80
REMARK 200 R MERGE FOR SHELL (I) : 3.02700
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 (%): 39.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, PEG 1000, PEG3350, AMINO ACIDS,
REMARK 280 MOPS, HEPES, 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: P 21 21 2
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 39.32150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.66250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.32150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.66250
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 431 LIES ON A SPECIAL POSITION.
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 SER A 3
REMARK 465 HIS A 4
REMARK 465 PRO A 5
REMARK 465 GLN A 6
REMARK 465 SER A 7
REMARK 465 THR A 8
REMARK 465 ARG A 9
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 PRO B 10
REMARK 465 ARG B 151
REMARK 465 SER B 152
REMARK 465 TRP B 153
REMARK 465 GLU B 154
REMARK 465 THR B 155
REMARK 465 TRP B 156
REMARK 465 LYS B 309
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 44 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 ARG B 185 NH1 - CZ - NH2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG B 185 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 LEU B 285 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
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 LEU A 27 -118.22 51.62
REMARK 500 SER A 29 -146.69 -128.43
REMARK 500 PRO A 54 46.14 -106.76
REMARK 500 THR A 55 -152.63 -98.77
REMARK 500 ASP A 120 -133.31 59.35
REMARK 500 GLU A 154 49.31 -78.46
REMARK 500 THR A 155 -18.04 -163.85
REMARK 500 ILE A 176 -63.05 -101.74
REMARK 500 GLU A 229 -80.15 -82.19
REMARK 500 PHE A 262 -59.92 -130.78
REMARK 500 LEU A 285 -128.89 -94.97
REMARK 500 ILE B 12 113.35 67.63
REMARK 500 LEU B 27 -128.27 59.46
REMARK 500 SER B 29 -149.43 -151.26
REMARK 500 PRO B 54 47.33 -106.26
REMARK 500 THR B 55 -155.34 -97.26
REMARK 500 PRO B 65 33.21 -68.03
REMARK 500 LYS B 109 67.45 33.81
REMARK 500 ASP B 120 -132.44 57.48
REMARK 500 ASP B 135 -66.38 11.24
REMARK 500 ARG B 185 -78.26 -143.82
REMARK 500 SER B 190 44.04 -104.91
REMARK 500 ARG B 193 128.67 166.04
REMARK 500 GLU B 229 -43.46 -133.57
REMARK 500 ALA B 247 30.09 -94.63
REMARK 500 SER B 248 101.63 -162.72
REMARK 500 ASP B 250 7.45 86.58
REMARK 500 PHE B 262 -61.79 -155.67
REMARK 500 SER B 264 -70.24 -45.48
REMARK 500 LYS B 265 42.59 -68.40
REMARK 500 ALA B 266 -14.10 -156.66
REMARK 500 GLU B 269 -83.23 -7.51
REMARK 500 LEU B 285 -125.28 -87.29
REMARK 500 SER B 292 59.00 -161.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO B 134 ASP B 135 142.16
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 151 0.23 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9RBP A 1 318 PDB 9RBP 9RBP 1 318
DBREF 9RBP B 1 318 PDB 9RBP 9RBP 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 501 10
HET PGE A 502 10
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 3 PGE 2(C6 H14 O4)
FORMUL 5 HOH *118(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 LEU A 108 1 16
HELIX 5 AA5 ASP A 120 HIS A 133 1 14
HELIX 6 AA6 PRO A 157 ARG A 168 1 12
HELIX 7 AA7 ALA A 171 LEU A 177 1 7
HELIX 8 AA8 ASN A 180 ARG A 185 1 6
HELIX 9 AA9 ARG A 185 SER A 190 1 6
HELIX 10 AB1 ARG A 196 GLU A 205 1 10
HELIX 11 AB2 PRO A 206 LYS A 208 5 3
HELIX 12 AB3 GLY A 211 SER A 213 5 3
HELIX 13 AB4 ARG A 214 ILE A 224 1 11
HELIX 14 AB5 PRO A 231 ALA A 247 1 17
HELIX 15 AB6 PHE A 263 TRP A 274 1 12
HELIX 16 AB7 PHE A 287 ASP A 291 5 5
HELIX 17 AB8 SER A 292 PHE A 308 1 17
HELIX 18 AB9 THR B 13 LYS B 20 1 8
HELIX 19 AC1 SER B 56 ARG B 61 5 6
HELIX 20 AC2 ILE B 63 PRO B 69 5 7
HELIX 21 AC3 ARG B 93 LYS B 109 1 17
HELIX 22 AC4 ASP B 120 HIS B 133 1 14
HELIX 23 AC5 ASP B 158 SER B 169 1 12
HELIX 24 AC6 ALA B 171 LEU B 177 1 7
HELIX 25 AC7 ASN B 180 ARG B 185 1 6
HELIX 26 AC8 ARG B 185 SER B 190 1 6
HELIX 27 AC9 ARG B 196 GLU B 205 1 10
HELIX 28 AD1 GLY B 211 SER B 213 5 3
HELIX 29 AD2 ARG B 214 GLU B 223 1 10
HELIX 30 AD3 PRO B 231 ALA B 247 1 17
HELIX 31 AD4 PHE B 263 TRP B 274 1 12
HELIX 32 AD5 PHE B 287 ASP B 291 5 5
HELIX 33 AD6 SER B 292 PHE B 308 1 17
SHEET 1 AA1 8 CYS A 21 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 CYS A 118
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 VAL A 282 N GLU A 257
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 ASN B 45 O ARG B 72
SHEET 5 AA2 8 ILE B 114 HIS B 119 1 O VAL B 117 N VAL B 48
SHEET 6 AA2 8 VAL B 137 MET B 143 1 O VAL B 141 N CYS B 118
SHEET 7 AA2 8 LYS B 253 ASP B 259 1 O ILE B 256 N HIS B 142
SHEET 8 AA2 8 THR B 277 LYS B 283 1 O LYS B 278 N LYS B 253
CISPEP 1 ASN A 53 PRO A 54 0 -3.48
CISPEP 2 GLY A 230 PRO A 231 0 -1.67
CISPEP 3 ASP A 259 PRO A 260 0 -1.73
CISPEP 4 ASN B 53 PRO B 54 0 -2.29
CISPEP 5 GLY B 230 PRO B 231 0 -9.48
CISPEP 6 ASP B 259 PRO B 260 0 5.03
CRYST1 78.643 81.325 93.689 90.00 90.00 90.00 P 21 21 2 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 0.012716 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012296 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010674 0.00000
TER 2452 LYS A 309
TER 4835 PHE B 308
MASTER 365 0 2 33 16 0 0 6 4963 2 20 50
END |