HEADER LUMINESCENT PROTEIN 26-AUG-03 1QV1
TITLE ATOMIC RESOLUTION STRUCTURE OF OBELIN FROM OBELIA LONGISSIMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OBELIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OBL;
COMPND 5 EC: 1.13.12.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OBELIA LONGISSIMA;
SOURCE 3 ORGANISM_TAXID: 32570;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET19-OL8
KEYWDS PHOTOPROTEIN, OBELIN, BIOLUMINESCENCE, ATOMIC RESOLUTION, CALCIUM
KEYWDS 2 BINDING, EF-HAND, LUMINESCENT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.J.LIU,E.S.VYSOTSKI,L.DENG,J.LEE,J.ROSE,B.C.WANG
REVDAT 6 16-AUG-23 1QV1 1 REMARK
REVDAT 5 27-OCT-21 1QV1 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 1QV1 1 VERSN
REVDAT 3 24-FEB-09 1QV1 1 VERSN
REVDAT 2 27-JAN-04 1QV1 1 JRNL
REVDAT 1 11-NOV-03 1QV1 0
JRNL AUTH Z.J.LIU,E.S.VYSOTSKI,L.DENG,J.LEE,J.ROSE,B.C.WANG
JRNL TITL ATOMIC RESOLUTION STRUCTURE OF OBELIN: SOAKING WITH CALCIUM
JRNL TITL 2 ENHANCES ELECTRON DENSITY OF THE SECOND OXYGEN ATOM
JRNL TITL 3 SUBSTITUTED AT THE C2-POSITION OF COELENTERAZINE.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 311 433 2003
JRNL REFN ISSN 0006-291X
JRNL PMID 14592432
JRNL DOI 10.1016/J.BBRC.2003.09.231
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.-J.LIU,E.VYSOTSKI,C.-J.CHEN,J.ROSE,J.LEE,B.-C.WANG
REMARK 1 TITL STRUCTURE OF THE CA2+-REGULATED PHOTOPROTEIN OBELIN AT 1.7
REMARK 1 TITL 2 RESOLUTION DETERMINED DIRECTLY FROM ITS SULFUR SUBSTRUCTURE
REMARK 1 REF PROTEIN SCI. V. 9 2085 2000
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.VYSOTSKI,Z.-J.LIU,J.ROSE,B.-C.WANG,J.LEE
REMARK 1 TITL PREPARATION AND PRELIMINARY STUDY OF CRYSTALS OF THE
REMARK 1 TITL 2 RECOMBINANT CALCIUM-REGULATED PHOTOPROTEIN OBELIN FROM THE
REMARK 1 TITL 3 BIOLUMINESCENT HYDROID OBELIA LONGISSIMA
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 55 1965 1999
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444999011828
REMARK 1 REFERENCE 3
REMARK 1 AUTH L.DENG,E.VYSOTSKI,Z.-J.LIU,S.MARKOVA,N.MALIKOVA,J.LEE,
REMARK 1 AUTH 2 J.ROSE,B.-C.WANG
REMARK 1 TITL STRUCTURAL BASIS FOR THE EMISSION OF VIOLET BIOLUMINESCENCE
REMARK 1 TITL 2 FROM A W92F OBELIN MUTANT
REMARK 1 REF FEBS LETT. V. 506 281 2001
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(01)02937-4
REMARK 1 REFERENCE 4
REMARK 1 AUTH E.VYSOTSKI,Z.-J.LIU,S.MARKOVA,J.BLINKS,L.DENG,L.FRANK,
REMARK 1 AUTH 2 M.HERKO,N.MALIKOVA,J.ROSE,B.-C.WANG,J.LEE
REMARK 1 TITL VIOLET BIOLUMINESCENCE AND FAST KINETICS FROM W92F OBELIN:
REMARK 1 TITL 2 STRUCTURE-BASED PROPOSALS FOR THE BIOLUMINESCENCE TRIGGERING
REMARK 1 TITL 3 AND THE IDENTIFICATION OF THE EMITTING SPECIES
REMARK 1 REF BIOCHEMISTRY V. 42 6013 2003
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI027258H
REMARK 2
REMARK 2 RESOLUTION. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.133
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.133
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.158
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 8.700
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 6968
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 86625
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.130
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.130
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.155
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 8.700
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 6639
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 75944
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1508
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 282
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1831.4
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1382.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 12
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 15459
REMARK 3 NUMBER OF RESTRAINTS : 18725
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 ANGLE DISTANCES (A) : 0.033
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.023
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.069
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.102
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.059
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.044
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R
REMARK 3 (NO CUTOFF) BY 0.0123
REMARK 4
REMARK 4 1QV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000020104.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93673
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.03400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.08900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1EL4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, POTASSIUM PHOSPHATE,
REMARK 280 HEXAMINECOBALTIC CHLORIDE , PH 5.8, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
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 41.66700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.31550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 41.66700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.31550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 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 A3204 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A3213 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 SER A 2
REMARK 465 SER A 3
REMARK 465 LYS A 4
REMARK 465 LYS A 124
REMARK 465 ASP A 125
REMARK 465 GLY A 126
REMARK 465 SER A 127
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 69 CD GLU A 69 OE2 0.071
REMARK 500
REMARK 500 REMARK: NULL
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 TYR A 5 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 TYR A 5 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 CYS A 75 CB - CA - C ANGL. DEV. = -18.7 DEGREES
REMARK 500 CYS A 75 CB - CA - C ANGL. DEV. = 10.2 DEGREES
REMARK 500 MET A 77 CA - CB - CG ANGL. DEV. = -12.0 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH2 ANGL. DEV. = -3.3 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 ASP A 12 57.54 -146.64
REMARK 500 ASP A 49 -72.38 -104.30
REMARK 500 SER A 145 73.44 -151.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 30 OD1
REMARK 620 2 ASN A 32 OD1 84.0
REMARK 620 3 ASN A 34 OD1 86.3 86.1
REMARK 620 4 LYS A 36 O 99.1 169.7 84.3
REMARK 620 5 HOH A3173 O 100.4 94.3 173.3 94.8
REMARK 620 6 HOH A3237 O 176.1 92.1 92.9 84.6 80.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 404 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 155 O
REMARK 620 2 ARG A 156 O 73.9
REMARK 620 3 CYS A 158 O 76.0 83.3
REMARK 620 4 HOH A3073 O 82.7 99.2 156.9
REMARK 620 5 HOH A3150 O 126.8 147.7 79.5 107.3
REMARK 620 6 HOH A3159 O 123.6 56.4 73.7 126.8 92.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CZH A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EL4 RELATED DB: PDB
REMARK 900 CONTAINS CALCIUM-REGULATED PHOTOPROTEIN OBELIN
REMARK 900 RELATED ID: 1EJ3 RELATED DB: PDB
REMARK 900 CONTAINS CALCIUM-REGULATED PHOTOPROTEIN AEQUORIN
REMARK 900 RELATED ID: 1JF0 RELATED DB: PDB
REMARK 900 CONTAINS CALCIUM-REGULATED PHOTOPROTEIN OBELIN
REMARK 900 RELATED ID: 1JF2 RELATED DB: PDB
REMARK 900 CONTAINS CALCIUM-REGULATED PHOTOPROTEIN OBELIN W92F MUTANT
REMARK 900 RELATED ID: 1QV0 RELATED DB: PDB
REMARK 900 CONTAINS CALCIUM-REGULATED PHOTOPROTEIN OBELIN
DBREF 1QV1 A 1 195 UNP Q27709 OBL_OBELO 1 195
SEQADV 1QV1 ALA A 163 UNP Q27709 SER 163 ENGINEERED MUTATION
SEQRES 1 A 195 MET SER SER LYS TYR ALA VAL LYS LEU LYS THR ASP PHE
SEQRES 2 A 195 ASP ASN PRO ARG TRP ILE LYS ARG HIS LYS HIS MET PHE
SEQRES 3 A 195 ASP PHE LEU ASP ILE ASN GLY ASN GLY LYS ILE THR LEU
SEQRES 4 A 195 ASP GLU ILE VAL SER LYS ALA SER ASP ASP ILE CYS ALA
SEQRES 5 A 195 LYS LEU GLU ALA THR PRO GLU GLN THR LYS ARG HIS GLN
SEQRES 6 A 195 VAL CYS VAL GLU ALA PHE PHE ARG GLY CYS GLY MET GLU
SEQRES 7 A 195 TYR GLY LYS GLU ILE ALA PHE PRO GLN PHE LEU ASP GLY
SEQRES 8 A 195 TRP LYS GLN LEU ALA THR SER GLU LEU LYS LYS TRP ALA
SEQRES 9 A 195 ARG ASN GLU PRO THR LEU ILE ARG GLU TRP GLY ASP ALA
SEQRES 10 A 195 VAL PHE ASP ILE PHE ASP LYS ASP GLY SER GLY THR ILE
SEQRES 11 A 195 THR LEU ASP GLU TRP LYS ALA TYR GLY LYS ILE SER GLY
SEQRES 12 A 195 ILE SER PRO SER GLN GLU ASP CYS GLU ALA THR PHE ARG
SEQRES 13 A 195 HIS CYS ASP LEU ASP ASN ALA GLY ASP LEU ASP VAL ASP
SEQRES 14 A 195 GLU MET THR ARG GLN HIS LEU GLY PHE TRP TYR THR LEU
SEQRES 15 A 195 ASP PRO GLU ALA ASP GLY LEU TYR GLY ASN GLY VAL PRO
HET CO A 401 1
HET CO A 402 1
HET CA A 403 1
HET K A 404 1
HET CZH A 201 34
HET GOL A 301 6
HETNAM CO COBALT (II) ION
HETNAM CA CALCIUM ION
HETNAM K POTASSIUM ION
HETNAM CZH C2-HYDROPEROXY-COELENTERAZINE
HETNAM GOL GLYCEROL
HETSYN CZH 8-BENZYL-2-HYDROPEROXY-2-(4-HYDROXY-BENZYL)-6-(4-
HETSYN 2 CZH HYDROXY-PHENYL)-2H-IMIDAZO[1,2-A]PYRAZIN-3-ONE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CO 2(CO 2+)
FORMUL 4 CA CA 2+
FORMUL 5 K K 1+
FORMUL 6 CZH C26 H21 N3 O5
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *282(H2 O)
HELIX 1 1 ASN A 15 ASP A 30 1 16
HELIX 2 2 THR A 38 ASP A 48 1 11
HELIX 3 3 ASP A 49 LEU A 54 1 6
HELIX 4 4 THR A 57 CYS A 75 1 19
HELIX 5 5 ALA A 84 ARG A 105 1 22
HELIX 6 6 THR A 109 PHE A 122 1 14
HELIX 7 7 THR A 131 GLY A 143 1 13
HELIX 8 8 SER A 147 CYS A 158 1 12
HELIX 9 9 VAL A 168 TYR A 180 1 13
HELIX 10 10 ASP A 183 ASP A 187 5 5
SHEET 1 A 2 THR A 129 ILE A 130 0
SHEET 2 A 2 LEU A 166 ASP A 167 -1 O LEU A 166 N ILE A 130
LINK OD1 ASP A 30 CA CA A 403 1555 1555 2.35
LINK OD1 ASN A 32 CA CA A 403 1555 1555 2.31
LINK OD1 ASN A 34 CA CA A 403 1555 1555 2.33
LINK O LYS A 36 CA CA A 403 1555 1555 2.31
LINK O PHE A 155 K K A 404 1555 1555 2.76
LINK O ARG A 156 K K A 404 1555 1555 2.91
LINK O CYS A 158 K K A 404 1555 1555 2.60
LINK CA CA A 403 O HOH A3173 1555 1555 2.36
LINK CA CA A 403 O HOH A3237 1555 1555 2.32
LINK K K A 404 O HOH A3073 1555 1555 2.89
LINK K K A 404 O HOH A3150 1555 1555 2.77
LINK K K A 404 O HOH A3159 1555 1555 2.24
SITE 1 AC1 6 ASP A 30 ASN A 32 ASN A 34 LYS A 36
SITE 2 AC1 6 HOH A3173 HOH A3237
SITE 1 AC2 6 PHE A 155 ARG A 156 CYS A 158 HOH A3073
SITE 2 AC2 6 HOH A3150 HOH A3159
SITE 1 AC3 16 HIS A 22 MET A 25 ILE A 42 ILE A 50
SITE 2 AC3 16 PHE A 88 TRP A 92 TRP A 114 GLY A 115
SITE 3 AC3 16 PHE A 119 TYR A 138 ILE A 144 MET A 171
SITE 4 AC3 16 HIS A 175 TRP A 179 TYR A 190 HOH A3042
SITE 1 AC4 7 HIS A 24 GLY A 143 ILE A 144 PRO A 146
SITE 2 AC4 7 GLY A 193 VAL A 194 HOH A3115
CRYST1 83.334 54.631 52.685 90.00 112.29 90.00 C 1 2 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 0.012000 0.000000 0.004919 0.00000
SCALE2 0.000000 0.018305 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020514 0.00000
(ATOM LINES ARE NOT SHOWN.)
END