HEADER LUMINESCENT PROTEIN 15-NOV-04 1VPR
TITLE CRYSTAL STRUCTURE OF A LUCIFERASE DOMAIN FROM THE
TITLE 2 DINOFLAGELLATE LINGULODINIUM POLYEDRUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LUCIFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 866-1241;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LINGULODINIUM POLYEDRUM;
SOURCE 3 ORGANISM_TAXID: 160621;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE-30
KEYWDS BETA BARREL, FATTY ACID BINDING PROTEIN, LIPOCALIN,
KEYWDS 2 LUCIFERASE, PH REGULATION, LUMINESCENT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.W.SCHULTZ,L.LIU,M.CEGIELSKI,J.W.HASTINGS
REVDAT 3 24-FEB-09 1VPR 1 VERSN
REVDAT 2 22-FEB-05 1VPR 1 JRNL
REVDAT 1 08-FEB-05 1VPR 0
JRNL AUTH L.W.SCHULTZ,L.LIU,M.CEGIELSKI,J.W.HASTINGS
JRNL TITL CRYSTAL STRUCTURE OF A PH-REGULATED LUCIFERASE
JRNL TITL 2 CATALYZING THE BIOLUMINESCENT OXIDATION OF AN OPEN
JRNL TITL 3 TETRAPYRROLE
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 1378 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15665092
JRNL DOI 10.1073/PNAS.0409335102
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.LIU,H.IM,M.CEGIELSKI,P.LEMAGUERES,L.W.SCHULTZ,
REMARK 1 AUTH 2 K.L.KRAUSE,J.W.HASTINGS
REMARK 1 TITL CHARACTERIZATION AND CRYSTALLIZATION OF ACTIVE
REMARK 1 TITL 2 DOMAINS OF A NOVEL LUCIFERASE FROM A MARINE
REMARK 1 TITL 3 DINOFLAGELLATE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 59 761 2003
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 12657805
REMARK 1 DOI 10.1107/S0907444903002920
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 35879
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM 8%
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5474
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 434
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2660
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 252
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.28
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.85
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE R-FACTOR THAT WAS CALCULATED
REMARK 3 USING SFCHECK (0.388) IS MUCH GREATER THAN THAT REPORTED BY
REMARK 3 THE AUTHOR (0.199). THE REASON FOR THIS DISCREPANCY IS THAT
REMARK 3 SOME RESIDUES, DUE TO LACK OF ELECTRON DENSITY, WERE MODELED
REMARK 3 AS ALANINE AND THE SIDE CHAINS WERE LATER ADDED AFTER
REMARK 3 REFINEMENT IN ORDER TO ACCOMODATE THE DEPOSITION.
REMARK 4
REMARK 4 1VPR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-04.
REMARK 100 THE RCSB ID CODE IS RCSB030961.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979070, 0.979259, 0.994904
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35921
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 55.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4000
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) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MEPEG 2000, 100MM EPPS, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
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 29.49450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.49300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.97750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.49300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.49450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.97750
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 300 REMARK: THIS IS A SINGLE DOMAIN FROM THE LUCIFERASE AND IS
REMARK 300 FUNCTIONAL AS A MONOMER.
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 VAL A 866
REMARK 465 CYS A 867
REMARK 465 GLY A 1219
REMARK 465 TRP A 1220
REMARK 465 LEU A 1221
REMARK 465 GLU A 1222
REMARK 465 LYS A 1223
REMARK 465 ASN A 1224
REMARK 465 GLU A 1225
REMARK 465 LYS A 1226
REMARK 465 GLU A 1227
REMARK 465 MET A 1228
REMARK 465 LEU A 1229
REMARK 465 ARG A 1230
REMARK 465 GLN A 1231
REMARK 465 ARG A 1232
REMARK 465 ASN A 1233
REMARK 465 ILE A 1234
REMARK 465 VAL A 1235
REMARK 465 SER A 1236
REMARK 465 SER A 1237
REMARK 465 THR A 1238
REMARK 465 PHE A 1239
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 GLU A 868 CG CD OE1 OE2
REMARK 470 LYS A 869 CG CD CE NZ
REMARK 470 LYS A 885 CG CD CE NZ
REMARK 470 GLU A 888 CG CD OE1 OE2
REMARK 470 LYS A 900 CG CD CE NZ
REMARK 470 GLU A 902 CG CD OE1 OE2
REMARK 470 HIS A 904 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 905 CG CD OE1 OE2
REMARK 470 ASP A 906 CG OD1 OD2
REMARK 470 LYS A 910 CG CD CE NZ
REMARK 470 LYS A 917 CG CD CE NZ
REMARK 470 LYS A 918 CG CD CE NZ
REMARK 470 GLU A 931 CG CD OE1 OE2
REMARK 470 GLU A 959 CG CD OE1 OE2
REMARK 470 LYS A 963 CG CD CE NZ
REMARK 470 LYS A1042 CG CD CE NZ
REMARK 470 LYS A1046 CG CD CE NZ
REMARK 470 SER A1047 OG
REMARK 470 MET A1049 CG SD CE
REMARK 470 LYS A1209 CG CD CE NZ
REMARK 470 LYS A1215 CG 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 TYR A 890 43.11 -99.87
REMARK 500 HIS A 904 135.12 -30.43
REMARK 500 ASN A 936 -178.06 -69.35
REMARK 500 CYS A 946 96.69 -165.57
REMARK 500 HIS A1064 -122.58 38.66
REMARK 500 LEU A1119 78.03 -119.87
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1VPR A 866 1239 UNP O77206 O77206_GONPO 866 1239
SEQADV 1VPR MSE A 898 UNP O77206 MET 898 MODIFIED RESIDUE
SEQADV 1VPR MSE A 912 UNP O77206 MET 912 MODIFIED RESIDUE
SEQADV 1VPR MSE A 957 UNP O77206 MET 957 MODIFIED RESIDUE
SEQADV 1VPR MSE A 990 UNP O77206 MET 990 MODIFIED RESIDUE
SEQADV 1VPR MSE A 1070 UNP O77206 MET 1070 MODIFIED RESIDUE
SEQADV 1VPR MSE A 1132 UNP O77206 MET 1132 MODIFIED RESIDUE
SEQADV 1VPR MSE A 1153 UNP O77206 MET 1153 MODIFIED RESIDUE
SEQRES 1 A 374 VAL CYS GLU LYS GLY PHE GLU ALA GLY ASP ASN LYS LEU
SEQRES 2 A 374 GLY GLY ALA LEU ASN ALA LYS HIS VAL GLU LYS TYR GLY
SEQRES 3 A 374 ASP ASN PHE LYS ASN GLY MSE HIS LYS PRO GLU PHE HIS
SEQRES 4 A 374 GLU ASP GLY LEU HIS LYS PRO MSE GLU VAL GLY GLY LYS
SEQRES 5 A 374 LYS PHE GLU SER GLY PHE HIS TYR LEU LEU GLU CYS HIS
SEQRES 6 A 374 GLU LEU GLY GLY LYS ASN ALA SER GLY GLY TYR GLY GLY
SEQRES 7 A 374 PRO LEU CYS GLU ASP PRO TYR GLY SER GLU VAL GLN ALA
SEQRES 8 A 374 MSE THR GLU LYS LEU LEU LYS GLU ALA ASP SER ASP ARG
SEQRES 9 A 374 THR LEU CYS PHE ASN ASN PHE GLN ASP PRO CYS PRO GLN
SEQRES 10 A 374 LEU THR LYS GLU GLN VAL ALA MSE CYS LYS GLY PHE ASP
SEQRES 11 A 374 TYR GLY ASP LYS THR LEU LYS LEU PRO CYS GLY PRO LEU
SEQRES 12 A 374 PRO TRP PRO ALA GLY LEU PRO GLU PRO GLY TYR VAL PRO
SEQRES 13 A 374 LYS THR ASN PRO LEU HIS GLY ARG TRP ILE THR VAL SER
SEQRES 14 A 374 GLY GLY GLN ALA ALA PHE ILE LYS GLU ALA ILE LYS SER
SEQRES 15 A 374 GLY MET LEU GLY ALA ALA GLU ALA ASN LYS ILE VAL ALA
SEQRES 16 A 374 ASP THR ASP HIS HIS GLN THR GLY GLY MSE TYR LEU ARG
SEQRES 17 A 374 ILE ASN GLN PHE GLY ASP VAL CYS THR VAL ASP ALA SER
SEQRES 18 A 374 VAL ALA LYS PHE ALA ARG ALA LYS ARG THR TRP LYS SER
SEQRES 19 A 374 GLY HIS TYR PHE TYR GLU PRO LEU VAL SER GLY GLY ASN
SEQRES 20 A 374 LEU LEU GLY VAL TRP VAL LEU PRO GLU GLU TYR ARG LYS
SEQRES 21 A 374 ILE GLY PHE PHE TRP GLU MSE GLU SER GLY ARG CYS PHE
SEQRES 22 A 374 ARG ILE GLU ARG ARG ALA PHE PRO VAL GLY PRO TYR THR
SEQRES 23 A 374 PHE MSE ARG GLN ALA THR GLU VAL GLY GLY LYS ILE SER
SEQRES 24 A 374 PHE VAL PHE TYR VAL LYS VAL SER ASN ASP PRO GLU SER
SEQRES 25 A 374 ASP PRO ILE PRO LEU GLN SER ARG ASP TYR THR ALA LEU
SEQRES 26 A 374 ALA GLY ARG ASP ASN ALA PRO THR ASN LEU GLY LYS PRO
SEQRES 27 A 374 TYR PRO THR LEU ALA LYS ASP LEU ASP TYR PRO LYS LYS
SEQRES 28 A 374 ARG ASP GLY TRP LEU GLU LYS ASN GLU LYS GLU MET LEU
SEQRES 29 A 374 ARG GLN ARG ASN ILE VAL SER SER THR PHE
MODRES 1VPR MSE A 898 MET SELENOMETHIONINE
MODRES 1VPR MSE A 912 MET SELENOMETHIONINE
MODRES 1VPR MSE A 957 MET SELENOMETHIONINE
MODRES 1VPR MSE A 990 MET SELENOMETHIONINE
MODRES 1VPR MSE A 1070 MET SELENOMETHIONINE
MODRES 1VPR MSE A 1132 MET SELENOMETHIONINE
MODRES 1VPR MSE A 1153 MET SELENOMETHIONINE
HET MSE A 898 8
HET MSE A 912 8
HET MSE A 957 8
HET MSE A 990 8
HET MSE A1070 8
HET MSE A1132 8
HET MSE A1153 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 2 HOH *252(H2 O)
HELIX 1 1 VAL A 887 ASP A 892 5 6
HELIX 2 2 SER A 921 GLU A 931 1 11
HELIX 3 3 GLY A 951 ASP A 966 1 16
HELIX 4 4 LEU A 971 GLN A 977 1 7
HELIX 5 5 THR A 984 LYS A 992 1 9
HELIX 6 6 GLY A 1036 SER A 1047 1 12
HELIX 7 7 GLY A 1051 ASP A 1063 1 13
HELIX 8 8 HIS A 1064 THR A 1067 5 4
HELIX 9 9 ARG A 1185 LEU A 1190 1 6
SHEET 1 A 2 PHE A 894 LYS A 895 0
SHEET 2 A 2 MSE A 898 HIS A 899 -1 O MSE A 898 N LYS A 895
SHEET 1 B 2 MSE A 912 VAL A 914 0
SHEET 2 B 2 LYS A 917 PHE A 919 -1 O PHE A 919 N MSE A 912
SHEET 1 C10 LYS A1094 LYS A1098 0
SHEET 2 C10 VAL A1080 ASP A1084 -1 N VAL A1083 O ARG A1095
SHEET 3 C10 TYR A1071 PHE A1077 -1 N PHE A1077 O VAL A1080
SHEET 4 C10 GLY A1028 SER A1034 -1 N TRP A1030 O LEU A1072
SHEET 5 C10 LYS A1162 SER A1172 -1 O PHE A1167 N VAL A1033
SHEET 6 C10 TYR A1150 VAL A1159 -1 N GLN A1155 O VAL A1166
SHEET 7 C10 CYS A1137 VAL A1147 -1 N PHE A1145 O PHE A1152
SHEET 8 C10 ARG A1124 GLU A1131 -1 N LYS A1125 O ARG A1142
SHEET 9 C10 ASN A1112 VAL A1118 -1 N LEU A1114 O TRP A1130
SHEET 10 C10 TYR A1102 PRO A1106 -1 N GLU A1105 O LEU A1113
LINK C GLY A 897 N MSE A 898 1555 1555 1.34
LINK C MSE A 898 N HIS A 899 1555 1555 1.34
LINK C PRO A 911 N MSE A 912 1555 1555 1.33
LINK C MSE A 912 N GLU A 913 1555 1555 1.32
LINK C ALA A 956 N MSE A 957 1555 1555 1.33
LINK C MSE A 957 N THR A 958 1555 1555 1.33
LINK C ALA A 989 N MSE A 990 1555 1555 1.33
LINK C MSE A 990 N CYS A 991 1555 1555 1.33
LINK C GLY A1069 N MSE A1070 1555 1555 1.33
LINK C MSE A1070 N TYR A1071 1555 1555 1.34
LINK C GLU A1131 N MSE A1132 1555 1555 1.33
LINK C MSE A1132 N GLU A1133 1555 1555 1.32
LINK C PHE A1152 N MSE A1153 1555 1555 1.32
LINK C MSE A1153 N ARG A1154 1555 1555 1.33
CISPEP 1 TYR A 1213 PRO A 1214 0 0.90
CRYST1 58.989 63.955 96.986 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 0.016952 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015636 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010311 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
