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HEADER OXIDOREDUCTASE 27-JAN-22 7QXQ
TITLE COELENTERAMIDE-BOUND RENILLA-TYPE LUCIFERASE (ANCFT)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRAGMENT TRANSPLANTATION ONTO HYPERSTABLE ANCESTOR OF
COMPND 3 HALOALKANE DEHALOGENASES AND RENILLA LUCIFERASE (ANC-FT);
COMPND 4 CHAIN: A, B, C;
COMPND 5 EC: 1.13.12.5;
COMPND 6 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, COELENTERAMIDE, RENILLA-LIKE, ENGINEERED ANCESTOR,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MAREK,A.SCHENKMAYEROVA
REVDAT 1 07-DEC-22 7QXQ 0
JRNL AUTH M.MAREK,A.SCHENKMAYEROVA
JRNL TITL COELENTERAMIDE-BOUND RENILLA-TYPE LUCIFERASE (ANCFT)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 38980
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 1920
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 44.8910 - 5.4211 1.00 2690 171 0.1627 0.1890
REMARK 3 2 5.4211 - 4.3040 1.00 2703 139 0.1372 0.1944
REMARK 3 3 4.3040 - 3.7603 0.99 2638 128 0.1517 0.2215
REMARK 3 4 3.7603 - 3.4166 0.99 2673 137 0.1730 0.2259
REMARK 3 5 3.4166 - 3.1718 1.00 2646 139 0.1701 0.2448
REMARK 3 6 3.1718 - 2.9848 1.00 2648 151 0.1864 0.2602
REMARK 3 7 2.9848 - 2.8354 1.00 2655 116 0.1907 0.2860
REMARK 3 8 2.8354 - 2.7120 1.00 2630 141 0.1827 0.2787
REMARK 3 9 2.7120 - 2.6076 1.00 2655 118 0.1942 0.2761
REMARK 3 10 2.6076 - 2.5176 1.00 2657 150 0.1831 0.2799
REMARK 3 11 2.5176 - 2.4389 1.00 2602 147 0.1787 0.2552
REMARK 3 12 2.4389 - 2.3692 1.00 2655 136 0.1789 0.2939
REMARK 3 13 2.3692 - 2.3068 1.00 2676 116 0.1910 0.3064
REMARK 3 14 2.3068 - 2.2510 0.98 2532 131 0.2434 0.3500
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.99
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 7QXQ 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_1292120603.
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 : 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-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75744
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 44.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
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 (%): 37.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM ACETATE, PEG 3350, PH 7.5,
REMARK 280 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 41.66600
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 MET A 1
REMARK 465 VAL A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 SER A 5
REMARK 465 GLN A 6
REMARK 465 ARG A 7
REMARK 465 THR A 8
REMARK 465 THR A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 SER B 5
REMARK 465 GLN B 6
REMARK 465 ARG B 7
REMARK 465 THR B 8
REMARK 465 THR B 9
REMARK 465 SER B 10
REMARK 465 THR B 11
REMARK 465 THR B 305
REMARK 465 LYS B 306
REMARK 465 HIS B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 SER C 3
REMARK 465 ALA C 4
REMARK 465 SER C 5
REMARK 465 GLN C 6
REMARK 465 ARG C 7
REMARK 465 THR C 8
REMARK 465 THR C 9
REMARK 465 SER C 10
REMARK 465 THR C 11
REMARK 465 ALA C 12
REMARK 465 HIS C 307
REMARK 465 HIS C 308
REMARK 465 HIS C 309
REMARK 465 HIS C 310
REMARK 465 HIS C 311
REMARK 465 HIS C 312
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 -130.85 47.54
REMARK 500 SER A 29 -156.45 -130.65
REMARK 500 PRO A 52 40.79 -107.58
REMARK 500 THR A 53 -158.69 -96.32
REMARK 500 ASP A 118 -136.25 60.71
REMARK 500 HIS A 131 58.18 -141.40
REMARK 500 GLU A 142 52.28 39.61
REMARK 500 ARG A 182 -53.32 -124.53
REMARK 500 ASP A 226 -19.86 -149.70
REMARK 500 SER A 245 59.88 -92.20
REMARK 500 PHE A 259 -73.99 -127.08
REMARK 500 LEU A 282 -132.38 -94.51
REMARK 500 PHE A 284 56.70 -92.05
REMARK 500 LEU B 27 -130.75 49.23
REMARK 500 SER B 29 -159.25 -119.51
REMARK 500 PRO B 52 48.34 -106.87
REMARK 500 THR B 53 -155.63 -107.58
REMARK 500 ASP B 118 -130.51 49.58
REMARK 500 GLU B 142 55.25 39.55
REMARK 500 ASP B 226 7.34 -153.10
REMARK 500 PHE B 259 -82.46 -129.23
REMARK 500 LEU B 282 -127.95 -86.22
REMARK 500 LEU C 27 -127.78 51.41
REMARK 500 HIS C 41 98.39 -42.22
REMARK 500 LYS C 42 5.42 -157.45
REMARK 500 ASN C 43 124.35 75.98
REMARK 500 PRO C 52 53.08 -109.06
REMARK 500 THR C 53 -152.43 -101.39
REMARK 500 ASP C 118 -131.14 61.82
REMARK 500 PHE C 259 -62.51 -131.28
REMARK 500 LEU C 282 -131.02 -103.22
REMARK 500 LEU C 304 77.77 -65.42
REMARK 500 THR C 305 -64.98 -130.60
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7QXQ A 1 312 PDB 7QXQ 7QXQ 1 312
DBREF 7QXQ B 1 312 PDB 7QXQ 7QXQ 1 312
DBREF 7QXQ C 1 312 PDB 7QXQ 7QXQ 1 312
SEQRES 1 A 312 MET VAL SER ALA SER GLN ARG THR THR SER THR ALA THR
SEQRES 2 A 312 GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN VAL ASP VAL
SEQRES 3 A 312 LEU ASP SER GLU MET SER TYR TYR ASP SER ASP PRO GLY
SEQRES 4 A 312 LYS HIS LYS ASN THR VAL ILE PHE LEU HIS GLY ASN PRO
SEQRES 5 A 312 THR SER SER TYR LEU TRP ARG ASN VAL ILE PRO HIS VAL
SEQRES 6 A 312 GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP LEU ILE GLY
SEQRES 7 A 312 MET GLY LYS SER GLY LYS LEU PRO ASN HIS SER TYR ARG
SEQRES 8 A 312 PHE VAL ASP HIS TYR ARG TYR LEU SER ALA TRP PHE ASP
SEQRES 9 A 312 SER VAL ASN LEU PRO GLU LYS VAL THR ILE VAL CYS HIS
SEQRES 10 A 312 ASP TRP GLY SER GLY LEU GLY PHE HIS TRP CYS ASN GLU
SEQRES 11 A 312 HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS MET GLU SER
SEQRES 12 A 312 VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP PRO ASP
SEQRES 13 A 312 ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU ALA GLY
SEQRES 14 A 312 GLU GLU MET VAL LEU LYS LYS ASN PHE PHE ILE GLU ARG
SEQRES 15 A 312 LEU LEU PRO SER SER ILE MET ARG LYS LEU SER GLU GLU
SEQRES 16 A 312 GLU MET ASP ALA TYR ARG GLU PRO PHE VAL GLU PRO GLY
SEQRES 17 A 312 GLU SER ARG ARG PRO THR LEU THR TRP PRO ARG GLU ILE
SEQRES 18 A 312 PRO ILE LYS GLY ASP GLY PRO GLU ASP VAL ILE GLU ILE
SEQRES 19 A 312 VAL LYS SER TYR ASN LYS TRP LEU SER THR SER LYS ASP
SEQRES 20 A 312 ILE PRO LYS LEU PHE ILE ASN ALA ASP PRO GLY PHE PHE
SEQRES 21 A 312 SER ASN ALA ILE LYS LYS VAL THR LYS ASN TRP PRO ASN
SEQRES 22 A 312 GLN LYS THR VAL THR VAL LYS GLY LEU HIS PHE LEU GLN
SEQRES 23 A 312 GLU ASP SER PRO GLU GLU ILE GLY GLU ALA ILE ALA ASP
SEQRES 24 A 312 PHE LEU ASN GLU LEU THR LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 312 MET VAL SER ALA SER GLN ARG THR THR SER THR ALA THR
SEQRES 2 B 312 GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN VAL ASP VAL
SEQRES 3 B 312 LEU ASP SER GLU MET SER TYR TYR ASP SER ASP PRO GLY
SEQRES 4 B 312 LYS HIS LYS ASN THR VAL ILE PHE LEU HIS GLY ASN PRO
SEQRES 5 B 312 THR SER SER TYR LEU TRP ARG ASN VAL ILE PRO HIS VAL
SEQRES 6 B 312 GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP LEU ILE GLY
SEQRES 7 B 312 MET GLY LYS SER GLY LYS LEU PRO ASN HIS SER TYR ARG
SEQRES 8 B 312 PHE VAL ASP HIS TYR ARG TYR LEU SER ALA TRP PHE ASP
SEQRES 9 B 312 SER VAL ASN LEU PRO GLU LYS VAL THR ILE VAL CYS HIS
SEQRES 10 B 312 ASP TRP GLY SER GLY LEU GLY PHE HIS TRP CYS ASN GLU
SEQRES 11 B 312 HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS MET GLU SER
SEQRES 12 B 312 VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP PRO ASP
SEQRES 13 B 312 ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU ALA GLY
SEQRES 14 B 312 GLU GLU MET VAL LEU LYS LYS ASN PHE PHE ILE GLU ARG
SEQRES 15 B 312 LEU LEU PRO SER SER ILE MET ARG LYS LEU SER GLU GLU
SEQRES 16 B 312 GLU MET ASP ALA TYR ARG GLU PRO PHE VAL GLU PRO GLY
SEQRES 17 B 312 GLU SER ARG ARG PRO THR LEU THR TRP PRO ARG GLU ILE
SEQRES 18 B 312 PRO ILE LYS GLY ASP GLY PRO GLU ASP VAL ILE GLU ILE
SEQRES 19 B 312 VAL LYS SER TYR ASN LYS TRP LEU SER THR SER LYS ASP
SEQRES 20 B 312 ILE PRO LYS LEU PHE ILE ASN ALA ASP PRO GLY PHE PHE
SEQRES 21 B 312 SER ASN ALA ILE LYS LYS VAL THR LYS ASN TRP PRO ASN
SEQRES 22 B 312 GLN LYS THR VAL THR VAL LYS GLY LEU HIS PHE LEU GLN
SEQRES 23 B 312 GLU ASP SER PRO GLU GLU ILE GLY GLU ALA ILE ALA ASP
SEQRES 24 B 312 PHE LEU ASN GLU LEU THR LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 312 MET VAL SER ALA SER GLN ARG THR THR SER THR ALA THR
SEQRES 2 C 312 GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN VAL ASP VAL
SEQRES 3 C 312 LEU ASP SER GLU MET SER TYR TYR ASP SER ASP PRO GLY
SEQRES 4 C 312 LYS HIS LYS ASN THR VAL ILE PHE LEU HIS GLY ASN PRO
SEQRES 5 C 312 THR SER SER TYR LEU TRP ARG ASN VAL ILE PRO HIS VAL
SEQRES 6 C 312 GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP LEU ILE GLY
SEQRES 7 C 312 MET GLY LYS SER GLY LYS LEU PRO ASN HIS SER TYR ARG
SEQRES 8 C 312 PHE VAL ASP HIS TYR ARG TYR LEU SER ALA TRP PHE ASP
SEQRES 9 C 312 SER VAL ASN LEU PRO GLU LYS VAL THR ILE VAL CYS HIS
SEQRES 10 C 312 ASP TRP GLY SER GLY LEU GLY PHE HIS TRP CYS ASN GLU
SEQRES 11 C 312 HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS MET GLU SER
SEQRES 12 C 312 VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP PRO ASP
SEQRES 13 C 312 ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU ALA GLY
SEQRES 14 C 312 GLU GLU MET VAL LEU LYS LYS ASN PHE PHE ILE GLU ARG
SEQRES 15 C 312 LEU LEU PRO SER SER ILE MET ARG LYS LEU SER GLU GLU
SEQRES 16 C 312 GLU MET ASP ALA TYR ARG GLU PRO PHE VAL GLU PRO GLY
SEQRES 17 C 312 GLU SER ARG ARG PRO THR LEU THR TRP PRO ARG GLU ILE
SEQRES 18 C 312 PRO ILE LYS GLY ASP GLY PRO GLU ASP VAL ILE GLU ILE
SEQRES 19 C 312 VAL LYS SER TYR ASN LYS TRP LEU SER THR SER LYS ASP
SEQRES 20 C 312 ILE PRO LYS LEU PHE ILE ASN ALA ASP PRO GLY PHE PHE
SEQRES 21 C 312 SER ASN ALA ILE LYS LYS VAL THR LYS ASN TRP PRO ASN
SEQRES 22 C 312 GLN LYS THR VAL THR VAL LYS GLY LEU HIS PHE LEU GLN
SEQRES 23 C 312 GLU ASP SER PRO GLU GLU ILE GLY GLU ALA ILE ALA ASP
SEQRES 24 C 312 PHE LEU ASN GLU LEU THR LYS HIS HIS HIS HIS HIS HIS
HET CEI A 400 31
HET CEI B 400 31
HET CEI C 400 31
HETNAM CEI N-[3-BENZYL-5-(4-HYDROXYPHENYL)PYRAZIN-2-YL]-2-(4-
HETNAM 2 CEI HYDROXYPHENYL)ACETAMIDE
HETSYN CEI COELENTERAMIDE
FORMUL 4 CEI 3(C25 H21 N3 O3)
FORMUL 7 HOH *275(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 ILE A 157 SER A 166 1 10
HELIX 7 AA7 GLU A 167 LEU A 174 1 8
HELIX 8 AA8 ASN A 177 ARG A 182 1 6
HELIX 9 AA9 ARG A 182 SER A 187 1 6
HELIX 10 AB1 SER A 193 GLU A 202 1 10
HELIX 11 AB2 PRO A 203 VAL A 205 5 3
HELIX 12 AB3 GLY A 208 SER A 210 5 3
HELIX 13 AB4 ARG A 211 GLU A 220 1 10
HELIX 14 AB5 PRO A 228 THR A 244 1 17
HELIX 15 AB6 PHE A 260 THR A 268 1 9
HELIX 16 AB7 PHE A 284 ASP A 288 5 5
HELIX 17 AB8 SER A 289 THR A 305 1 17
HELIX 18 AB9 THR B 13 ALA B 19 1 7
HELIX 19 AC1 SER B 54 ARG B 59 5 6
HELIX 20 AC2 VAL B 61 VAL B 65 5 5
HELIX 21 AC3 ARG B 91 SER B 105 1 15
HELIX 22 AC4 ASP B 118 HIS B 131 1 14
HELIX 23 AC5 SER B 150 TRP B 154 5 5
HELIX 24 AC6 ILE B 157 SER B 166 1 10
HELIX 25 AC7 SER B 166 LYS B 175 1 10
HELIX 26 AC8 ASN B 177 ARG B 182 1 6
HELIX 27 AC9 ARG B 182 SER B 187 1 6
HELIX 28 AD1 SER B 193 GLU B 202 1 10
HELIX 29 AD2 PRO B 203 VAL B 205 5 3
HELIX 30 AD3 GLY B 208 SER B 210 5 3
HELIX 31 AD4 ARG B 211 GLU B 220 1 10
HELIX 32 AD5 PRO B 228 THR B 244 1 17
HELIX 33 AD6 PHE B 260 THR B 268 1 9
HELIX 34 AD7 PHE B 284 ASP B 288 5 5
HELIX 35 AD8 SER B 289 GLU B 303 1 15
HELIX 36 AD9 GLY C 14 LYS C 20 1 7
HELIX 37 AE1 SER C 54 ARG C 59 5 6
HELIX 38 AE2 VAL C 61 VAL C 65 5 5
HELIX 39 AE3 ARG C 91 VAL C 106 1 16
HELIX 40 AE4 ASP C 118 HIS C 131 1 14
HELIX 41 AE5 SER C 150 TRP C 154 5 5
HELIX 42 AE6 ILE C 157 LYS C 165 1 9
HELIX 43 AE7 SER C 166 LYS C 175 1 10
HELIX 44 AE8 ASN C 177 ARG C 182 1 6
HELIX 45 AE9 ARG C 182 SER C 187 1 6
HELIX 46 AF1 SER C 193 GLU C 202 1 10
HELIX 47 AF2 PRO C 203 VAL C 205 5 3
HELIX 48 AF3 GLY C 208 SER C 210 5 3
HELIX 49 AF4 ARG C 211 GLU C 220 1 10
HELIX 50 AF5 PRO C 228 THR C 244 1 17
HELIX 51 AF6 PHE C 260 THR C 268 1 9
HELIX 52 AF7 PHE C 284 ASP C 288 5 5
HELIX 53 AF8 SER C 289 LEU C 304 1 16
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 LYS A 136 N VAL A 112
SHEET 7 AA1 8 LYS A 250 PRO A 257 1 O LEU A 251 N HIS A 140
SHEET 8 AA1 8 GLN A 274 GLY A 281 1 O VAL A 277 N ASN A 254
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 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 250 PRO B 257 1 O LEU B 251 N ILE B 138
SHEET 8 AA2 8 GLN B 274 GLY B 281 1 O VAL B 279 N ASP B 256
SHEET 1 AA3 8 CYS C 21 VAL C 26 0
SHEET 2 AA3 8 SER C 29 ASP C 35 -1 O SER C 29 N VAL C 26
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 VAL C 45 O ARG C 70
SHEET 5 AA3 8 VAL C 112 HIS C 117 1 O VAL C 115 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 VAL C 277 N ASN C 254
CISPEP 1 ASN A 51 PRO A 52 0 5.39
CISPEP 2 ASP A 256 PRO A 257 0 4.49
CISPEP 3 ASN B 51 PRO B 52 0 0.50
CISPEP 4 ASP B 256 PRO B 257 0 -0.48
CISPEP 5 ASN C 51 PRO C 52 0 -2.71
CISPEP 6 GLY C 227 PRO C 228 0 -12.99
CISPEP 7 ASP C 256 PRO C 257 0 3.34
CRYST1 49.224 83.332 102.017 90.00 91.89 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 0.020315 0.000000 0.000669 0.00000
SCALE2 0.000000 0.012000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009808 0.00000
TER 2478 HIS A 312
TER 4871 LEU B 304
TER 7264 LYS C 306
MASTER 311 0 3 53 24 0 0 6 7598 3 93 72
END |