HEADER OXIDOREDUCTASE 31-AUG-05 2D1T
TITLE CRYSTAL STRUCTURE OF THE THERMOSTABLE JAPANESE FIREFLY LUCIFERASE RED-
TITLE 2 COLOR EMISSION S286N MUTANT COMPLEXED WITH HIGH-ENERGY INTERMEDIATE
TITLE 3 ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LUCIFERIN 4-MONOOXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LUCIFERASE;
COMPND 5 EC: 1.13.12.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LUCIOLA CRUCIATA;
SOURCE 3 ORGANISM_COMMON: JAPANESE FIREFLY;
SOURCE 4 ORGANISM_TAXID: 7051;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PUC18
KEYWDS ALPHA/BETA, BETA BARREL, ALPHA+BETA, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.NAKATSU,S.ICHIYAMA,J.HIRATAKE,A.SALDANHA,N.KOBASHI,K.SAKATA,H.KATO,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 6 15-NOV-23 2D1T 1 REMARK
REVDAT 5 25-OCT-23 2D1T 1 REMARK
REVDAT 4 10-NOV-21 2D1T 1 REMARK SEQADV
REVDAT 3 25-DEC-19 2D1T 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2D1T 1 VERSN
REVDAT 1 21-MAR-06 2D1T 0
JRNL AUTH T.NAKATSU,S.ICHIYAMA,J.HIRATAKE,A.SALDANHA,N.KOBASHI,
JRNL AUTH 2 K.SAKATA,H.KATO
JRNL TITL STRUCTURAL BASIS FOR THE SPECTRAL DIFFERENCE IN LUCIFERASE
JRNL TITL 2 BIOLUMINESCENCE.
JRNL REF NATURE V. 440 372 2006
JRNL REFN ISSN 0028-0836
JRNL PMID 16541080
JRNL DOI 10.1038/NATURE04542
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 90068
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4734
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6285
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 313
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4111
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 843
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : 0.44000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.064
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.036
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.922
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4254 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5775 ; 1.381 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 538 ; 5.701 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 670 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3141 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2134 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 639 ; 0.125 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 38 ; 0.158 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 48 ; 0.112 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2672 ; 0.651 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4342 ; 1.176 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1582 ; 1.909 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1433 ; 3.070 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D1T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000024882.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-02
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94838
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2D1S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, LITHIUM CHROLIDE, MAGNESIUM
REMARK 280 CHLORIDE, HEPES, 5'-O-[N-(DEHYDROLUCIFERYL)-SULFAMOYL] ADENOSINE,
REMARK 280 PH 7.8, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 28.73400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.11950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.58700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 26.11950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.73400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 90.58700
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 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 GLU A 2
REMARK 465 ASN A 3
REMARK 465 MET A 4
REMARK 465 GLU A 5
REMARK 465 ASN A 6
REMARK 465 ALA A 546
REMARK 465 LYS A 547
REMARK 465 MET A 548
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 15 CE NZ
REMARK 470 GLU A 22 CD OE1 OE2
REMARK 470 GLU A 34 OE1 OE2
REMARK 470 LYS A 38 CD CE NZ
REMARK 470 TYR A 178 OH
REMARK 470 GLN A 179 CD OE1 NE2
REMARK 470 LYS A 299 CD CE NZ
REMARK 470 LYS A 305 CD CE NZ
REMARK 470 LYS A 382 CD CE NZ
REMARK 470 ARG A 388 NH1 NH2
REMARK 470 GLU A 408 CD OE1 OE2
REMARK 470 LYS A 411 CD CE NZ
REMARK 470 GLU A 412 CG CD OE1 OE2
REMARK 470 LYS A 445 CE NZ
REMARK 470 GLU A 539 CD OE1 OE2
REMARK 470 LYS A 543 CD CE NZ
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 SER A 234 108.36 -168.37
REMARK 500 THR A 348 -66.25 68.71
REMARK 500 LEU A 370 -3.10 77.89
REMARK 500 ASN A 406 68.62 -150.74
REMARK 500 ASP A 438 -179.72 -174.53
REMARK 500 LYS A 447 -130.04 49.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SLU A 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2D1R RELATED DB: PDB
REMARK 900 T217I MUTANT WITH OLU
REMARK 900 RELATED ID: 2D1S RELATED DB: PDB
REMARK 900 T217I MUTANT WITH SLU
REMARK 900 RELATED ID: MY_001000084.4 RELATED DB: TARGETDB
DBREF 2D1T A 4 548 UNP P13129 LUCI_LUCCR 4 548
SEQADV 2D1T MET A 1 UNP P13129 DELETION
SEQADV 2D1T GLU A 2 UNP P13129 DELETION
SEQADV 2D1T ASN A 3 UNP P13129 DELETION
SEQADV 2D1T CSO A 64 UNP P13129 CYS 64 MODIFIED RESIDUE
SEQADV 2D1T ILE A 217 UNP P13129 THR 217 ENGINEERED MUTATION
SEQADV 2D1T ASN A 286 UNP P13129 SER 286 ENGINEERED MUTATION
SEQRES 1 A 548 MET GLU ASN MET GLU ASN ASP GLU ASN ILE VAL VAL GLY
SEQRES 2 A 548 PRO LYS PRO PHE TYR PRO ILE GLU GLU GLY SER ALA GLY
SEQRES 3 A 548 THR GLN LEU ARG LYS TYR MET GLU ARG TYR ALA LYS LEU
SEQRES 4 A 548 GLY ALA ILE ALA PHE THR ASN ALA VAL THR GLY VAL ASP
SEQRES 5 A 548 TYR SER TYR ALA GLU TYR LEU GLU LYS SER CYS CSO LEU
SEQRES 6 A 548 GLY LYS ALA LEU GLN ASN TYR GLY LEU VAL VAL ASP GLY
SEQRES 7 A 548 ARG ILE ALA LEU CYS SER GLU ASN CYS GLU GLU PHE PHE
SEQRES 8 A 548 ILE PRO VAL ILE ALA GLY LEU PHE ILE GLY VAL GLY VAL
SEQRES 9 A 548 ALA PRO THR ASN GLU ILE TYR THR LEU ARG GLU LEU VAL
SEQRES 10 A 548 HIS SER LEU GLY ILE SER LYS PRO THR ILE VAL PHE SER
SEQRES 11 A 548 SER LYS LYS GLY LEU ASP LYS VAL ILE THR VAL GLN LYS
SEQRES 12 A 548 THR VAL THR THR ILE LYS THR ILE VAL ILE LEU ASP SER
SEQRES 13 A 548 LYS VAL ASP TYR ARG GLY TYR GLN CYS LEU ASP THR PHE
SEQRES 14 A 548 ILE LYS ARG ASN THR PRO PRO GLY TYR GLN ALA SER SER
SEQRES 15 A 548 PHE LYS THR VAL GLU VAL ASP ARG LYS GLU GLN VAL ALA
SEQRES 16 A 548 LEU ILE MET ASN SER SER GLY SER THR GLY LEU PRO LYS
SEQRES 17 A 548 GLY VAL GLN LEU THR HIS GLU ASN ILE VAL THR ARG PHE
SEQRES 18 A 548 SER HIS ALA ARG ASP PRO ILE TYR GLY ASN GLN VAL SER
SEQRES 19 A 548 PRO GLY THR ALA VAL LEU THR VAL VAL PRO PHE HIS HIS
SEQRES 20 A 548 GLY PHE GLY MET PHE THR THR LEU GLY TYR LEU ILE CYS
SEQRES 21 A 548 GLY PHE ARG VAL VAL MET LEU THR LYS PHE ASP GLU GLU
SEQRES 22 A 548 THR PHE LEU LYS THR LEU GLN ASP TYR LYS CYS THR ASN
SEQRES 23 A 548 VAL ILE LEU VAL PRO THR LEU PHE ALA ILE LEU ASN LYS
SEQRES 24 A 548 SER GLU LEU LEU ASN LYS TYR ASP LEU SER ASN LEU VAL
SEQRES 25 A 548 GLU ILE ALA SER GLY GLY ALA PRO LEU SER LYS GLU VAL
SEQRES 26 A 548 GLY GLU ALA VAL ALA ARG ARG PHE ASN LEU PRO GLY VAL
SEQRES 27 A 548 ARG GLN GLY TYR GLY LEU THR GLU THR THR SER ALA ILE
SEQRES 28 A 548 ILE ILE THR PRO GLU GLY ASP ASP LYS PRO GLY ALA SER
SEQRES 29 A 548 GLY LYS VAL VAL PRO LEU PHE LYS ALA LYS VAL ILE ASP
SEQRES 30 A 548 LEU ASP THR LYS LYS SER LEU GLY PRO ASN ARG ARG GLY
SEQRES 31 A 548 GLU VAL CYS VAL LYS GLY PRO MET LEU MET LYS GLY TYR
SEQRES 32 A 548 VAL ASN ASN PRO GLU ALA THR LYS GLU LEU ILE ASP GLU
SEQRES 33 A 548 GLU GLY TRP LEU HIS THR GLY ASP ILE GLY TYR TYR ASP
SEQRES 34 A 548 GLU GLU LYS HIS PHE PHE ILE VAL ASP ARG LEU LYS SER
SEQRES 35 A 548 LEU ILE LYS TYR LYS GLY TYR GLN VAL PRO PRO ALA GLU
SEQRES 36 A 548 LEU GLU SER VAL LEU LEU GLN HIS PRO SER ILE PHE ASP
SEQRES 37 A 548 ALA GLY VAL ALA GLY VAL PRO ASP PRO VAL ALA GLY GLU
SEQRES 38 A 548 LEU PRO GLY ALA VAL VAL VAL LEU GLU SER GLY LYS ASN
SEQRES 39 A 548 MET THR GLU LYS GLU VAL MET ASP TYR VAL ALA SER GLN
SEQRES 40 A 548 VAL SER ASN ALA LYS ARG LEU ARG GLY GLY VAL ARG PHE
SEQRES 41 A 548 VAL ASP GLU VAL PRO LYS GLY LEU THR GLY LYS ILE ASP
SEQRES 42 A 548 GLY ARG ALA ILE ARG GLU ILE LEU LYS LYS PRO VAL ALA
SEQRES 43 A 548 LYS MET
MODRES 2D1T CSO A 64 CYS S-HYDROXYCYSTEINE
HET CSO A 64 7
HET CL A1001 1
HET CL A1002 1
HET SLU A2001 40
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM CL CHLORIDE ION
HETNAM SLU 5'-O-[N-(DEHYDROLUCIFERYL)-SULFAMOYL] ADENOSINE
FORMUL 1 CSO C3 H7 N O3 S
FORMUL 2 CL 2(CL 1-)
FORMUL 4 SLU C21 H18 N8 O8 S3
FORMUL 5 HOH *843(H2 O)
HELIX 1 1 SER A 24 GLY A 40 1 17
HELIX 2 2 TYR A 55 GLY A 73 1 19
HELIX 3 3 PHE A 90 GLY A 101 1 12
HELIX 4 4 THR A 112 LYS A 124 1 13
HELIX 5 5 GLY A 134 VAL A 145 1 12
HELIX 6 6 CYS A 165 ASN A 173 1 9
HELIX 7 7 GLN A 179 PHE A 183 5 5
HELIX 8 8 HIS A 214 ARG A 225 1 12
HELIX 9 9 HIS A 247 GLY A 261 1 15
HELIX 10 10 ASP A 271 TYR A 282 1 12
HELIX 11 11 VAL A 290 THR A 292 5 3
HELIX 12 12 LEU A 293 SER A 300 1 8
HELIX 13 13 LEU A 302 TYR A 306 5 5
HELIX 14 14 SER A 322 PHE A 333 1 12
HELIX 15 15 THR A 345 THR A 348 5 4
HELIX 16 16 ASN A 406 ILE A 414 1 9
HELIX 17 17 LYS A 441 LEU A 443 5 3
HELIX 18 18 PRO A 452 GLN A 462 1 11
HELIX 19 19 THR A 496 SER A 506 1 11
HELIX 20 20 SER A 509 ARG A 513 5 5
HELIX 21 21 ASP A 533 LYS A 543 1 11
SHEET 1 A 5 VAL A 11 VAL A 12 0
SHEET 2 A 5 LYS A 372 ILE A 376 -1 O ALA A 373 N VAL A 11
SHEET 3 A 5 GLY A 390 LYS A 395 -1 O CYS A 393 N LYS A 374
SHEET 4 A 5 LEU A 420 TYR A 428 -1 O LEU A 420 N VAL A 394
SHEET 5 A 5 PHE A 434 ARG A 439 -1 O ASP A 438 N ILE A 425
SHEET 1 B 9 ASP A 52 SER A 54 0
SHEET 2 B 9 ILE A 42 ASN A 46 -1 N PHE A 44 O TYR A 53
SHEET 3 B 9 ARG A 263 MET A 266 1 O VAL A 264 N ALA A 43
SHEET 4 B 9 ALA A 238 THR A 241 1 N VAL A 239 O VAL A 265
SHEET 5 B 9 ASN A 286 LEU A 289 1 O ASN A 286 N LEU A 240
SHEET 6 B 9 GLU A 313 GLY A 317 1 O ALA A 315 N VAL A 287
SHEET 7 B 9 ARG A 339 GLY A 343 1 O ARG A 339 N ILE A 314
SHEET 8 B 9 ALA A 350 ILE A 353 -1 O ILE A 351 N TYR A 342
SHEET 9 B 9 LYS A 366 VAL A 367 -1 O LYS A 366 N ILE A 353
SHEET 1 C 4 GLY A 103 THR A 107 0
SHEET 2 C 4 ARG A 79 CYS A 83 1 N ILE A 80 O GLY A 103
SHEET 3 C 4 ILE A 127 SER A 130 1 O PHE A 129 N ALA A 81
SHEET 4 C 4 THR A 150 ILE A 153 1 O VAL A 152 N VAL A 128
SHEET 1 D 3 VAL A 194 MET A 198 0
SHEET 2 D 3 VAL A 210 THR A 213 -1 O LEU A 212 N ALA A 195
SHEET 3 D 3 GLY A 402 TYR A 403 -1 O GLY A 402 N GLN A 211
SHEET 1 E 3 ILE A 466 ASP A 476 0
SHEET 2 E 3 GLY A 480 LEU A 489 -1 O LEU A 482 N VAL A 474
SHEET 3 E 3 VAL A 518 PHE A 520 1 O ARG A 519 N VAL A 487
LINK C CYS A 63 N CSO A 64 1555 1555 1.33
LINK C CSO A 64 N LEU A 65 1555 1555 1.33
SITE 1 AC1 6 SER A 201 GLY A 527 LEU A 528 THR A 529
SITE 2 AC1 6 GLY A 530 LYS A 531
SITE 1 AC2 5 SER A 201 GLY A 202 GLY A 527 LEU A 528
SITE 2 AC2 5 HOH A2139
SITE 1 AC3 25 SER A 200 SER A 201 HIS A 247 PHE A 249
SITE 2 AC3 25 THR A 253 ILE A 288 GLY A 318 ALA A 319
SITE 3 AC3 25 PRO A 320 GLN A 340 GLY A 341 TYR A 342
SITE 4 AC3 25 GLY A 343 LEU A 344 THR A 345 ALA A 350
SITE 5 AC3 25 ASP A 424 ARG A 439 LYS A 531 HOH A2002
SITE 6 AC3 25 HOH A2007 HOH A2099 HOH A2101 HOH A2172
SITE 7 AC3 25 HOH A2537
CRYST1 57.468 181.174 52.239 90.00 90.00 90.00 P 21 21 21 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 0.017401 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019143 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
