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HEADER OXIDOREDUCTASE 27-JAN-22 7QXR
TITLE AZACOELENTERAZINE-BOUND RENILLA-TYPE LUCIFERASE (ANCFT)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRAGMENT TRANSPLANTATION ONTO A HYPERSTABLE ANCESTOR OF
COMPND 3 HALOALKANE DEHALOGENASES AND RENILLA LUCIFERASE (ANC-FT);
COMPND 4 CHAIN: A, B, C;
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 LUCIFERASE, AZACOELENTERAZINE, SUBSTRATE ANALOGUE, RENILLA-LIKE,
KEYWDS 2 ENGINEERED ANCESTOR, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAREK,A.SCHENKMAYEROVA,Y.L.JANIN
REVDAT 1 07-DEC-22 7QXR 0
JRNL AUTH M.MAREK,A.SCHENKMAYEROVA
JRNL TITL AZACOELENTERAZINE-BOUND RENILLA-TYPE LUCIFERASE (ANCFT)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.05 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 56384
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2852
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 46.9440 - 5.5667 1.00 2784 137 0.1638 0.2059
REMARK 3 2 5.5667 - 4.4195 1.00 2686 171 0.1401 0.1759
REMARK 3 3 4.4195 - 3.8611 1.00 2704 136 0.1448 0.1846
REMARK 3 4 3.8611 - 3.5082 1.00 2676 172 0.1738 0.2300
REMARK 3 5 3.5082 - 3.2569 0.99 2678 146 0.1857 0.2457
REMARK 3 6 3.2569 - 3.0649 1.00 2696 125 0.1953 0.2379
REMARK 3 7 3.0649 - 2.9114 1.00 2726 126 0.2103 0.3106
REMARK 3 8 2.9114 - 2.7847 0.99 2697 134 0.2057 0.2494
REMARK 3 9 2.7847 - 2.6775 1.00 2663 127 0.2139 0.2904
REMARK 3 10 2.6775 - 2.5851 1.00 2660 151 0.2285 0.2985
REMARK 3 11 2.5851 - 2.5043 1.00 2672 152 0.2368 0.3421
REMARK 3 12 2.5043 - 2.4327 0.99 2665 140 0.2276 0.3144
REMARK 3 13 2.4327 - 2.3687 1.00 2660 152 0.2379 0.3243
REMARK 3 14 2.3687 - 2.3109 0.99 2665 152 0.2324 0.3363
REMARK 3 15 2.3109 - 2.2583 0.99 2642 162 0.2475 0.3333
REMARK 3 16 2.2583 - 2.2103 0.99 2645 162 0.2593 0.3035
REMARK 3 17 2.2103 - 2.1661 0.99 2689 129 0.2576 0.3129
REMARK 3 18 2.1661 - 2.1252 0.99 2646 136 0.2753 0.3424
REMARK 3 19 2.1252 - 2.0872 0.99 2701 115 0.2869 0.3377
REMARK 3 20 2.0872 - 2.0520 0.97 2577 127 0.2997 0.3056
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.44
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 : 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 7QXR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292120604.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56440
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 46.944
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 6S97
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM CHLORIDE, BIS-TRIS, PEG
REMARK 280 3350, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
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 43.77450
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, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 THR B 11
REMARK 465 THR B 305
REMARK 465 THR C 305
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 -133.59 53.78
REMARK 500 SER A 29 -153.29 -126.30
REMARK 500 PRO A 52 41.39 -107.34
REMARK 500 THR A 53 -152.11 -96.17
REMARK 500 ASP A 118 -132.08 56.03
REMARK 500 VAL A 173 -64.92 -93.52
REMARK 500 PHE A 259 -68.87 -129.02
REMARK 500 LEU A 282 -132.22 -98.07
REMARK 500 PHE A 284 56.96 -91.18
REMARK 500 LEU B 27 -127.21 48.14
REMARK 500 SER B 29 -154.34 -127.84
REMARK 500 LYS B 40 76.00 46.42
REMARK 500 LYS B 42 166.61 178.41
REMARK 500 PRO B 52 46.32 -108.49
REMARK 500 THR B 53 -155.06 -96.68
REMARK 500 ASN B 107 71.53 60.03
REMARK 500 ASP B 118 -134.25 53.37
REMARK 500 HIS B 131 48.64 -140.66
REMARK 500 ASP B 226 26.07 -152.54
REMARK 500 PHE B 259 -73.00 -124.39
REMARK 500 LEU B 282 -125.57 -97.18
REMARK 500 LEU C 27 -128.91 44.20
REMARK 500 SER C 29 -145.70 -118.71
REMARK 500 HIS C 41 31.15 -85.93
REMARK 500 PRO C 52 48.59 -106.62
REMARK 500 THR C 53 -157.21 -103.95
REMARK 500 TYR C 90 50.47 -118.57
REMARK 500 ASP C 118 -137.25 58.84
REMARK 500 HIS C 131 50.83 -145.39
REMARK 500 ASP C 226 -31.17 -152.64
REMARK 500 SER C 245 70.08 -69.68
REMARK 500 PHE C 259 -73.04 -128.24
REMARK 500 LEU C 282 -131.86 -93.96
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 590 DISTANCE = 6.97 ANGSTROMS
DBREF 7QXR A 11 305 PDB 7QXR 7QXR 11 305
DBREF 7QXR B 11 305 PDB 7QXR 7QXR 11 305
DBREF 7QXR C 11 305 PDB 7QXR 7QXR 11 305
SEQRES 1 A 295 THR ALA THR GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN
SEQRES 2 A 295 VAL ASP VAL LEU ASP SER GLU MET SER TYR TYR ASP SER
SEQRES 3 A 295 ASP PRO GLY LYS HIS LYS ASN THR VAL ILE PHE LEU HIS
SEQRES 4 A 295 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE
SEQRES 5 A 295 PRO HIS VAL GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP
SEQRES 6 A 295 LEU ILE GLY MET GLY LYS SER GLY LYS LEU PRO ASN HIS
SEQRES 7 A 295 SER TYR ARG PHE VAL ASP HIS TYR ARG TYR LEU SER ALA
SEQRES 8 A 295 TRP PHE ASP SER VAL ASN LEU PRO GLU LYS VAL THR ILE
SEQRES 9 A 295 VAL CYS HIS ASP TRP GLY SER GLY LEU GLY PHE HIS TRP
SEQRES 10 A 295 CYS ASN GLU HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS
SEQRES 11 A 295 MET GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU
SEQRES 12 A 295 TRP PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER
SEQRES 13 A 295 GLU ALA GLY GLU GLU MET VAL LEU LYS LYS ASN PHE PHE
SEQRES 14 A 295 ILE GLU ARG LEU LEU PRO SER SER ILE MET ARG LYS LEU
SEQRES 15 A 295 SER GLU GLU GLU MET ASP ALA TYR ARG GLU PRO PHE VAL
SEQRES 16 A 295 GLU PRO GLY GLU SER ARG ARG PRO THR LEU THR TRP PRO
SEQRES 17 A 295 ARG GLU ILE PRO ILE LYS GLY ASP GLY PRO GLU ASP VAL
SEQRES 18 A 295 ILE GLU ILE VAL LYS SER TYR ASN LYS TRP LEU SER THR
SEQRES 19 A 295 SER LYS ASP ILE PRO LYS LEU PHE ILE ASN ALA ASP PRO
SEQRES 20 A 295 GLY PHE PHE SER ASN ALA ILE LYS LYS VAL THR LYS ASN
SEQRES 21 A 295 TRP PRO ASN GLN LYS THR VAL THR VAL LYS GLY LEU HIS
SEQRES 22 A 295 PHE LEU GLN GLU ASP SER PRO GLU GLU ILE GLY GLU ALA
SEQRES 23 A 295 ILE ALA ASP PHE LEU ASN GLU LEU THR
SEQRES 1 B 295 THR ALA THR GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN
SEQRES 2 B 295 VAL ASP VAL LEU ASP SER GLU MET SER TYR TYR ASP SER
SEQRES 3 B 295 ASP PRO GLY LYS HIS LYS ASN THR VAL ILE PHE LEU HIS
SEQRES 4 B 295 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE
SEQRES 5 B 295 PRO HIS VAL GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP
SEQRES 6 B 295 LEU ILE GLY MET GLY LYS SER GLY LYS LEU PRO ASN HIS
SEQRES 7 B 295 SER TYR ARG PHE VAL ASP HIS TYR ARG TYR LEU SER ALA
SEQRES 8 B 295 TRP PHE ASP SER VAL ASN LEU PRO GLU LYS VAL THR ILE
SEQRES 9 B 295 VAL CYS HIS ASP TRP GLY SER GLY LEU GLY PHE HIS TRP
SEQRES 10 B 295 CYS ASN GLU HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS
SEQRES 11 B 295 MET GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU
SEQRES 12 B 295 TRP PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER
SEQRES 13 B 295 GLU ALA GLY GLU GLU MET VAL LEU LYS LYS ASN PHE PHE
SEQRES 14 B 295 ILE GLU ARG LEU LEU PRO SER SER ILE MET ARG LYS LEU
SEQRES 15 B 295 SER GLU GLU GLU MET ASP ALA TYR ARG GLU PRO PHE VAL
SEQRES 16 B 295 GLU PRO GLY GLU SER ARG ARG PRO THR LEU THR TRP PRO
SEQRES 17 B 295 ARG GLU ILE PRO ILE LYS GLY ASP GLY PRO GLU ASP VAL
SEQRES 18 B 295 ILE GLU ILE VAL LYS SER TYR ASN LYS TRP LEU SER THR
SEQRES 19 B 295 SER LYS ASP ILE PRO LYS LEU PHE ILE ASN ALA ASP PRO
SEQRES 20 B 295 GLY PHE PHE SER ASN ALA ILE LYS LYS VAL THR LYS ASN
SEQRES 21 B 295 TRP PRO ASN GLN LYS THR VAL THR VAL LYS GLY LEU HIS
SEQRES 22 B 295 PHE LEU GLN GLU ASP SER PRO GLU GLU ILE GLY GLU ALA
SEQRES 23 B 295 ILE ALA ASP PHE LEU ASN GLU LEU THR
SEQRES 1 C 295 THR ALA THR GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN
SEQRES 2 C 295 VAL ASP VAL LEU ASP SER GLU MET SER TYR TYR ASP SER
SEQRES 3 C 295 ASP PRO GLY LYS HIS LYS ASN THR VAL ILE PHE LEU HIS
SEQRES 4 C 295 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN VAL ILE
SEQRES 5 C 295 PRO HIS VAL GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP
SEQRES 6 C 295 LEU ILE GLY MET GLY LYS SER GLY LYS LEU PRO ASN HIS
SEQRES 7 C 295 SER TYR ARG PHE VAL ASP HIS TYR ARG TYR LEU SER ALA
SEQRES 8 C 295 TRP PHE ASP SER VAL ASN LEU PRO GLU LYS VAL THR ILE
SEQRES 9 C 295 VAL CYS HIS ASP TRP GLY SER GLY LEU GLY PHE HIS TRP
SEQRES 10 C 295 CYS ASN GLU HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS
SEQRES 11 C 295 MET GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU
SEQRES 12 C 295 TRP PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER
SEQRES 13 C 295 GLU ALA GLY GLU GLU MET VAL LEU LYS LYS ASN PHE PHE
SEQRES 14 C 295 ILE GLU ARG LEU LEU PRO SER SER ILE MET ARG LYS LEU
SEQRES 15 C 295 SER GLU GLU GLU MET ASP ALA TYR ARG GLU PRO PHE VAL
SEQRES 16 C 295 GLU PRO GLY GLU SER ARG ARG PRO THR LEU THR TRP PRO
SEQRES 17 C 295 ARG GLU ILE PRO ILE LYS GLY ASP GLY PRO GLU ASP VAL
SEQRES 18 C 295 ILE GLU ILE VAL LYS SER TYR ASN LYS TRP LEU SER THR
SEQRES 19 C 295 SER LYS ASP ILE PRO LYS LEU PHE ILE ASN ALA ASP PRO
SEQRES 20 C 295 GLY PHE PHE SER ASN ALA ILE LYS LYS VAL THR LYS ASN
SEQRES 21 C 295 TRP PRO ASN GLN LYS THR VAL THR VAL LYS GLY LEU HIS
SEQRES 22 C 295 PHE LEU GLN GLU ASP SER PRO GLU GLU ILE GLY GLU ALA
SEQRES 23 C 295 ILE ALA ASP PHE LEU ASN GLU LEU THR
HET NSW A 401 32
HET NSW B 401 32
HET NSW C 401 32
HETNAM NSW 3-(4-HYDROXYPHENYL)-8-[(4-HYDROXYPHENYL)METHYL]-5-
HETNAM 2 NSW (PHENYLMETHYL)-1$L^{4},4,7,8-
HETNAM 3 NSW TETRAZABICYCLO[4.3.0]NONA-1(6),2,4-TRIEN-9-ONE
FORMUL 4 NSW 3(C25 H21 N4 O3 1+)
FORMUL 7 HOH *303(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 SER A 150 TRP A 154 5 5
HELIX 7 AA7 ILE A 157 SER A 166 1 10
HELIX 8 AA8 GLU A 167 LEU A 174 1 8
HELIX 9 AA9 ASN A 177 ARG A 182 1 6
HELIX 10 AB1 ARG A 182 SER A 187 1 6
HELIX 11 AB2 SER A 193 GLU A 202 1 10
HELIX 12 AB3 PRO A 203 VAL A 205 5 3
HELIX 13 AB4 GLY A 208 SER A 210 5 3
HELIX 14 AB5 ARG A 211 GLU A 220 1 10
HELIX 15 AB6 PRO A 228 SER A 243 1 16
HELIX 16 AB7 PHE A 260 THR A 268 1 9
HELIX 17 AB8 PHE A 284 ASP A 288 5 5
HELIX 18 AB9 SER A 289 LEU A 304 1 16
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 VAL B 65 5 5
HELIX 22 AC4 ARG B 91 ASP B 104 1 14
HELIX 23 AC5 ASP B 118 GLU B 130 1 13
HELIX 24 AC6 HIS B 131 ASP B 133 5 3
HELIX 25 AC7 SER B 150 TRP B 154 5 5
HELIX 26 AC8 ILE B 157 SER B 166 1 10
HELIX 27 AC9 SER B 166 LYS B 175 1 10
HELIX 28 AD1 ASN B 177 ARG B 182 1 6
HELIX 29 AD2 ARG B 182 SER B 187 1 6
HELIX 30 AD3 SER B 193 GLU B 202 1 10
HELIX 31 AD4 PRO B 203 VAL B 205 5 3
HELIX 32 AD5 GLY B 208 SER B 210 5 3
HELIX 33 AD6 ARG B 211 GLU B 220 1 10
HELIX 34 AD7 PRO B 228 THR B 244 1 17
HELIX 35 AD8 PHE B 260 THR B 268 1 9
HELIX 36 AD9 PHE B 284 ASP B 288 5 5
HELIX 37 AE1 SER B 289 GLU B 303 1 15
HELIX 38 AE2 THR C 13 ALA C 19 1 7
HELIX 39 AE3 SER C 54 ARG C 59 5 6
HELIX 40 AE4 VAL C 61 ALA C 69 5 9
HELIX 41 AE5 ARG C 91 ASP C 104 1 14
HELIX 42 AE6 ASP C 118 HIS C 131 1 14
HELIX 43 AE7 SER C 150 TRP C 154 5 5
HELIX 44 AE8 ILE C 157 SER C 166 1 10
HELIX 45 AE9 SER C 166 LYS C 175 1 10
HELIX 46 AF1 ASN C 177 ARG C 182 1 6
HELIX 47 AF2 ARG C 182 SER C 187 1 6
HELIX 48 AF3 SER C 193 GLU C 202 1 10
HELIX 49 AF4 PRO C 203 VAL C 205 5 3
HELIX 50 AF5 GLY C 208 SER C 210 5 3
HELIX 51 AF6 ARG C 211 GLU C 220 1 10
HELIX 52 AF7 PRO C 228 THR C 244 1 17
HELIX 53 AF8 PHE C 260 THR C 268 1 9
HELIX 54 AF9 PHE C 284 ASP C 288 5 5
HELIX 55 AG1 SER C 289 GLU C 303 1 15
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 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 LYS A 136 N VAL A 112
SHEET 7 AA1 8 LYS A 250 PRO A 257 1 O ILE A 253 N HIS A 140
SHEET 8 AA1 8 GLN A 274 GLY A 281 1 O LYS A 275 N PHE A 252
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 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 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 250 PRO B 257 1 O LEU B 251 N HIS B 140
SHEET 8 AA2 8 GLN B 274 GLY B 281 1 O LYS B 275 N PHE B 252
SHEET 1 AA3 8 LYS C 22 VAL C 26 0
SHEET 2 AA3 8 SER C 29 ASP C 35 -1 O TYR C 33 N LYS C 22
SHEET 3 AA3 8 ARG C 70 PRO C 74 -1 O ALA C 73 N TYR C 34
SHEET 4 AA3 8 THR C 44 LEU C 48 1 N PHE C 47 O LEU C 72
SHEET 5 AA3 8 VAL C 112 HIS C 117 1 O THR C 113 N ILE C 46
SHEET 6 AA3 8 VAL C 135 MET C 141 1 O LYS C 136 N VAL C 112
SHEET 7 AA3 8 LYS C 250 PRO C 257 1 O LEU C 251 N HIS C 140
SHEET 8 AA3 8 GLN C 274 GLY C 281 1 O LYS C 275 N PHE C 252
CISPEP 1 ASN A 51 PRO A 52 0 1.36
CISPEP 2 ASP A 256 PRO A 257 0 9.67
CISPEP 3 ASN B 51 PRO B 52 0 -0.21
CISPEP 4 ASP B 256 PRO B 257 0 4.29
CISPEP 5 ASN C 51 PRO C 52 0 5.03
CISPEP 6 ASP C 256 PRO C 257 0 0.23
CRYST1 51.284 87.549 102.693 90.00 93.46 90.00 P 1 21 1 6
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 0.019499 0.000000 0.001180 0.00000
SCALE2 0.000000 0.011422 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009756 0.00000
TER 2396 THR A 305
TER 4778 LEU B 304
TER 7175 LEU C 304
MASTER 285 0 3 55 24 0 0 6 7563 3 96 69
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