HEADER OXIDOREDUCTASE 21-SEP-04 1XI2
TITLE QUINONE REDUCTASE 2 IN COMPLEX WITH CANCER PRODRUG CB1954
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NRH DEHYDROGENASE [QUINONE] 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: QUINONE REDUCTASE 2, QR2, NRH:QUINONE OXIDOREDUCTASE 2;
COMPND 5 EC: 1.6.99.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NQO2, NMOR2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS QR2, CB1954, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.FU,L.BURYANOVSKYY,Z.ZHANG
REVDAT 6 14-FEB-24 1XI2 1 REMARK HETSYN LINK
REVDAT 5 12-DEC-18 1XI2 1 HETSYN
REVDAT 4 19-JAN-11 1XI2 1 REMARK
REVDAT 3 24-FEB-09 1XI2 1 VERSN
REVDAT 2 13-SEP-05 1XI2 1 JRNL
REVDAT 1 30-AUG-05 1XI2 0
JRNL AUTH Y.FU,L.BURYANOVSKYY,Z.ZHANG
JRNL TITL CRYSTAL STRUCTURE OF QUINONE REDUCTASE 2 IN COMPLEX WITH
JRNL TITL 2 CANCER PRODRUG CB1954
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 336 332 2005
JRNL REFN ISSN 0006-291X
JRNL PMID 16129418
JRNL DOI 10.1016/J.BBRC.2005.08.081
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.20
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 78011
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 SET) : 0.216
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 7833
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 3648
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 145
REMARK 3 SOLVENT ATOMS : 362
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.10
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) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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: NULL
REMARK 4
REMARK 4 1XI2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030387.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : 1.00
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78011
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 35.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
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 <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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 288K
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 41.73750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.34500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.22750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 28.34500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.73750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.22750
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ASN A 61 81.69 -168.58
REMARK 500 PRO A 62 6.84 -69.46
REMARK 500 TYR A 132 -128.59 58.17
REMARK 500 TYR A 155 51.09 -91.99
REMARK 500 ALA A 191 65.49 27.70
REMARK 500 CYS A 222 79.02 -68.20
REMARK 500 ARG B 78 48.40 72.04
REMARK 500 TYR B 132 -125.49 55.53
REMARK 500 TYR B 155 51.00 -96.30
REMARK 500 ALA B 191 61.49 33.68
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 ZN A 231 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 173 ND1
REMARK 620 2 HIS A 177 ND1 110.9
REMARK 620 3 CYS A 222 SG 124.2 113.7
REMARK 620 4 CYS A 222 O 110.6 94.5 97.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 232 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 173 ND1
REMARK 620 2 HIS B 177 ND1 106.2
REMARK 620 3 CYS B 222 SG 126.4 114.8
REMARK 620 4 CYS B 222 O 110.5 99.2 95.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 432
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1233
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 1234
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CB1 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CB1 B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QR2 RELATED DB: PDB
REMARK 900 APO-PROTEIN STRUCTURE
REMARK 900 RELATED ID: 2QR2 RELATED DB: PDB
REMARK 900 QR2 IN COMPLEX WITH MENADIONE
DBREF 1XI2 A 1 230 UNP P16083 NQO2_HUMAN 1 230
DBREF 1XI2 B 1 230 UNP P16083 NQO2_HUMAN 1 230
SEQRES 1 A 230 ALA GLY LYS LYS VAL LEU ILE VAL TYR ALA HIS GLN GLU
SEQRES 2 A 230 PRO LYS SER PHE ASN GLY SER LEU LYS ASN VAL ALA VAL
SEQRES 3 A 230 ASP GLU LEU SER ARG GLN GLY CYS THR VAL THR VAL SER
SEQRES 4 A 230 ASP LEU TYR ALA MET ASN PHE GLU PRO ARG ALA THR ASP
SEQRES 5 A 230 LYS ASP ILE THR GLY THR LEU SER ASN PRO GLU VAL PHE
SEQRES 6 A 230 ASN TYR GLY VAL GLU THR HIS GLU ALA TYR LYS GLN ARG
SEQRES 7 A 230 SER LEU ALA SER ASP ILE THR ASP GLU GLN LYS LYS VAL
SEQRES 8 A 230 ARG GLU ALA ASP LEU VAL ILE PHE GLN PHE PRO LEU TYR
SEQRES 9 A 230 TRP PHE SER VAL PRO ALA ILE LEU LYS GLY TRP MET ASP
SEQRES 10 A 230 ARG VAL LEU CYS GLN GLY PHE ALA PHE ASP ILE PRO GLY
SEQRES 11 A 230 PHE TYR ASP SER GLY LEU LEU GLN GLY LYS LEU ALA LEU
SEQRES 12 A 230 LEU SER VAL THR THR GLY GLY THR ALA GLU MET TYR THR
SEQRES 13 A 230 LYS THR GLY VAL ASN GLY ASP SER ARG TYR PHE LEU TRP
SEQRES 14 A 230 PRO LEU GLN HIS GLY THR LEU HIS PHE CYS GLY PHE LYS
SEQRES 15 A 230 VAL LEU ALA PRO GLN ILE SER PHE ALA PRO GLU ILE ALA
SEQRES 16 A 230 SER GLU GLU GLU ARG LYS GLY MET VAL ALA ALA TRP SER
SEQRES 17 A 230 GLN ARG LEU GLN THR ILE TRP LYS GLU GLU PRO ILE PRO
SEQRES 18 A 230 CYS THR ALA HIS TRP HIS PHE GLY GLN
SEQRES 1 B 230 ALA GLY LYS LYS VAL LEU ILE VAL TYR ALA HIS GLN GLU
SEQRES 2 B 230 PRO LYS SER PHE ASN GLY SER LEU LYS ASN VAL ALA VAL
SEQRES 3 B 230 ASP GLU LEU SER ARG GLN GLY CYS THR VAL THR VAL SER
SEQRES 4 B 230 ASP LEU TYR ALA MET ASN PHE GLU PRO ARG ALA THR ASP
SEQRES 5 B 230 LYS ASP ILE THR GLY THR LEU SER ASN PRO GLU VAL PHE
SEQRES 6 B 230 ASN TYR GLY VAL GLU THR HIS GLU ALA TYR LYS GLN ARG
SEQRES 7 B 230 SER LEU ALA SER ASP ILE THR ASP GLU GLN LYS LYS VAL
SEQRES 8 B 230 ARG GLU ALA ASP LEU VAL ILE PHE GLN PHE PRO LEU TYR
SEQRES 9 B 230 TRP PHE SER VAL PRO ALA ILE LEU LYS GLY TRP MET ASP
SEQRES 10 B 230 ARG VAL LEU CYS GLN GLY PHE ALA PHE ASP ILE PRO GLY
SEQRES 11 B 230 PHE TYR ASP SER GLY LEU LEU GLN GLY LYS LEU ALA LEU
SEQRES 12 B 230 LEU SER VAL THR THR GLY GLY THR ALA GLU MET TYR THR
SEQRES 13 B 230 LYS THR GLY VAL ASN GLY ASP SER ARG TYR PHE LEU TRP
SEQRES 14 B 230 PRO LEU GLN HIS GLY THR LEU HIS PHE CYS GLY PHE LYS
SEQRES 15 B 230 VAL LEU ALA PRO GLN ILE SER PHE ALA PRO GLU ILE ALA
SEQRES 16 B 230 SER GLU GLU GLU ARG LYS GLY MET VAL ALA ALA TRP SER
SEQRES 17 B 230 GLN ARG LEU GLN THR ILE TRP LYS GLU GLU PRO ILE PRO
SEQRES 18 B 230 CYS THR ALA HIS TRP HIS PHE GLY GLN
HET ZN A 231 1
HET FAD A1234 53
HET CB1 A 501 18
HET ZN B 232 1
HET ZN B 432 1
HET FAD B1233 53
HET CB1 B 502 18
HETNAM ZN ZINC ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM CB1 5-(AZIRIDIN-1-YL)-2,4-DINITROBENZAMIDE
HETSYN CB1 CB1954; TRETAZICAR
FORMUL 3 ZN 3(ZN 2+)
FORMUL 4 FAD 2(C27 H33 N9 O15 P2)
FORMUL 5 CB1 2(C9 H8 N4 O5)
FORMUL 10 HOH *362(H2 O)
HELIX 1 1 SER A 16 GLN A 32 1 17
HELIX 2 2 THR A 51 ILE A 55 5 5
HELIX 3 3 ASN A 66 GLN A 77 1 12
HELIX 4 4 ALA A 81 ALA A 94 1 14
HELIX 5 5 PRO A 109 LEU A 120 1 12
HELIX 6 6 PHE A 131 GLY A 135 5 5
HELIX 7 7 ASP A 163 HIS A 173 1 11
HELIX 8 8 SER A 196 THR A 213 1 18
HELIX 9 9 ILE A 214 GLU A 217 5 4
HELIX 10 10 THR A 223 PHE A 228 1 6
HELIX 11 11 SER B 16 GLN B 32 1 17
HELIX 12 12 THR B 51 ILE B 55 5 5
HELIX 13 13 ASN B 66 ARG B 78 1 13
HELIX 14 14 ALA B 81 ALA B 94 1 14
HELIX 15 15 PRO B 109 LEU B 120 1 12
HELIX 16 16 PHE B 131 GLY B 135 5 5
HELIX 17 17 ALA B 152 THR B 156 5 5
HELIX 18 18 ASP B 163 HIS B 173 1 11
HELIX 19 19 SER B 196 THR B 213 1 18
HELIX 20 20 ILE B 214 GLU B 217 5 4
HELIX 21 21 THR B 223 GLY B 229 1 7
SHEET 1 A 5 THR A 35 ASP A 40 0
SHEET 2 A 5 LYS A 4 TYR A 9 1 N VAL A 5 O THR A 35
SHEET 3 A 5 LEU A 96 PRO A 102 1 O ILE A 98 N VAL A 8
SHEET 4 A 5 LEU A 141 THR A 147 1 O SER A 145 N PHE A 99
SHEET 5 A 5 LYS A 182 VAL A 183 1 O LYS A 182 N ALA A 142
SHEET 1 B 5 THR A 35 ASP A 40 0
SHEET 2 B 5 LYS A 4 TYR A 9 1 N VAL A 5 O THR A 35
SHEET 3 B 5 LEU A 96 PRO A 102 1 O ILE A 98 N VAL A 8
SHEET 4 B 5 LEU A 141 THR A 147 1 O SER A 145 N PHE A 99
SHEET 5 B 5 GLN A 187 SER A 189 1 O GLN A 187 N LEU A 144
SHEET 1 C 5 THR B 35 ASP B 40 0
SHEET 2 C 5 LYS B 4 TYR B 9 1 N VAL B 5 O THR B 35
SHEET 3 C 5 LEU B 96 PRO B 102 1 O ILE B 98 N LEU B 6
SHEET 4 C 5 LEU B 141 THR B 147 1 O SER B 145 N PHE B 99
SHEET 5 C 5 LYS B 182 VAL B 183 1 O LYS B 182 N ALA B 142
SHEET 1 D 5 THR B 35 ASP B 40 0
SHEET 2 D 5 LYS B 4 TYR B 9 1 N VAL B 5 O THR B 35
SHEET 3 D 5 LEU B 96 PRO B 102 1 O ILE B 98 N LEU B 6
SHEET 4 D 5 LEU B 141 THR B 147 1 O SER B 145 N PHE B 99
SHEET 5 D 5 GLN B 187 SER B 189 1 O SER B 189 N VAL B 146
LINK ND1 HIS A 173 ZN ZN A 231 1555 1555 2.17
LINK ND1 HIS A 177 ZN ZN A 231 1555 1555 2.20
LINK SG CYS A 222 ZN ZN A 231 1555 1555 2.38
LINK O CYS A 222 ZN ZN A 231 1555 1555 2.20
LINK ND1 HIS B 173 ZN ZN B 232 1555 1555 2.13
LINK ND1 HIS B 177 ZN ZN B 232 1555 1555 2.17
LINK SG CYS B 222 ZN ZN B 232 1555 1555 2.34
LINK O CYS B 222 ZN ZN B 232 1555 1555 2.13
LINK N THR B 223 ZN ZN B 432 1555 1555 2.72
CISPEP 1 ILE B 128 PRO B 129 0 -0.06
SITE 1 AC1 3 HIS A 173 HIS A 177 CYS A 222
SITE 1 AC2 4 HIS B 173 HIS B 177 CYS B 222 ZN B 432
SITE 1 AC3 6 TRP B 169 HIS B 173 CYS B 222 THR B 223
SITE 2 AC3 6 HIS B 227 ZN B 232
SITE 1 AC4 29 ASN A 66 ASP A 117 HIS B 11 LYS B 15
SITE 2 AC4 29 SER B 16 PHE B 17 ASN B 18 SER B 20
SITE 3 AC4 29 PRO B 102 LEU B 103 TYR B 104 TRP B 105
SITE 4 AC4 29 PHE B 106 THR B 147 THR B 148 GLY B 149
SITE 5 AC4 29 GLY B 150 TYR B 155 PRO B 192 GLU B 193
SITE 6 AC4 29 GLU B 197 ARG B 200 CB1 B 502 HOH B1288
SITE 7 AC4 29 HOH B1337 HOH B1339 HOH B1376 HOH B1377
SITE 8 AC4 29 HOH B1430
SITE 1 AC5 25 HIS A 11 LYS A 15 SER A 16 PHE A 17
SITE 2 AC5 25 ASN A 18 SER A 20 PRO A 102 LEU A 103
SITE 3 AC5 25 TYR A 104 TRP A 105 PHE A 106 THR A 147
SITE 4 AC5 25 THR A 148 GLY A 149 GLY A 150 TYR A 155
SITE 5 AC5 25 GLU A 193 ARG A 200 CB1 A 501 HOH A1286
SITE 6 AC5 25 HOH A1323 HOH A1331 HOH A1358 ASN B 66
SITE 7 AC5 25 ASP B 117
SITE 1 AC6 9 TRP A 105 GLY A 149 GLY A 150 ASN A 161
SITE 2 AC6 9 FAD A1234 PHE B 126 ILE B 128 PHE B 178
SITE 3 AC6 9 HOH B1395
SITE 1 AC7 9 PHE A 126 PHE A 178 HOH A1363 TRP B 105
SITE 2 AC7 9 GLY B 149 GLY B 150 ASN B 161 FAD B1233
SITE 3 AC7 9 HOH B1430
CRYST1 83.475 106.455 56.690 90.00 90.00 90.00 P 21 21 21 8
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 0.011980 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009394 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
