HEADER BILIVERDIN-IX BETA REDUCTASE 19-NOV-00 1HE5
TITLE HUMAN BILIVERDIN IX BETA REDUCTASE: NADP/LUMICHROME TERNARY COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILIVERDIN IX BETA REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FLAVIN REDUCTASE (EC 1.6.99.1), NADPH-DEPENDENT DIAPHORASE,
COMPND 5 NADPH-FLAVIN REDUCTASE, BILIVERDIN REDUCTASE B, GREEN HEME BINDING
COMPND 6 PROTEIN;
COMPND 7 EC: 1.3.1.24;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BILIVERDIN-IX BETA REDUCTASE, FOETAL METABOLISM, HAEM DEGRADATION,
KEYWDS 2 FLAVIN REDUCTASE, DIAPHORASE, GREEN HAEM BINDING PROTEIN,
KEYWDS 3 METHAEMOGLOBIN REDUCTASE, ALPHA/BETA DINUCLEOTIDE BINDING FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.B.PEREIRA,S.MACEDO-RIBEIRO,A.PARRAGA,R.PEREZ-LUQUE,O.CUNNINGHAM,
AUTHOR 2 K.DARCY,T.J.MANTLE,M.COLL
REVDAT 4 13-DEC-23 1HE5 1 REMARK
REVDAT 3 22-MAY-19 1HE5 1 REMARK ATOM
REVDAT 2 24-FEB-09 1HE5 1 VERSN
REVDAT 1 28-FEB-01 1HE5 0
JRNL AUTH P.J.B.PEREIRA,S.MACEDO-RIBEIRO,A.PARRAGA,R.PEREZ-LUQUE,
JRNL AUTH 2 O.CUNNINGHAM,K.DARCY,T.J.MANTLE,M.COLL
JRNL TITL STRUCTURE OF HUMAN BILIVERDIN IX BETA REDUCTASE, AN EARLY
JRNL TITL 2 FETAL BILIRUBIN IX PRODUCING ENZYME
JRNL REF NAT.STRUCT.BIOL. V. 8 215 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11224564
JRNL DOI 10.1038/84948
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
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) : 0.148
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.143
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1739
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 34700
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.145
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.140
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1598
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 31850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1540
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 271
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1841.8
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 11
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 17257
REMARK 3 NUMBER OF RESTRAINTS : 20960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 ANGLE DISTANCES (A) : 0.022
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.049
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.067
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.011
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.001
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.018
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.079
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HE5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1290005568.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9310
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34757
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 44.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.7000
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) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.14900
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: AMORE
REMARK 200 STARTING MODEL: 1HDO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0.2 M AMMONIUM SULFATE,
REMARK 280 0.1 M SODIUM CACODYLATE PH 6.5. NADP ADDED TO A FINAL
REMARK 280 CONCENTRATION OF 2.5 MM, PH 6.50
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 20.05000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.45000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.45000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.05000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.60000
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: BIOLOGICAL_UNIT: 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 GLN A 206
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 MET A 1 CG SD CE
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 4 CG CD CE NZ
REMARK 480 ARG A 39 CZ NH1 NH2
REMARK 480 LYS A 120 CB CG CD CE NZ
REMARK 480 ARG A 124 CD NE CZ NH1 NH2
REMARK 480 ARG A 174 CD NE CZ NH1 NH2
REMARK 480 ARG A 187 CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CE LYS A 4 O HOH A 2056 1.77
REMARK 500 NH2 ARG A 39 NH2 ARG A 78 2.10
REMARK 500 CD LYS A 4 O HOH A 2056 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG A 124 NE2 GLN A 204 4545 2.18
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 146 CB - CG - CD1 ANGL. DEV. = 3.7 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 ARG A 78 -122.27 49.61
REMARK 500 THR A 110 -106.12 -117.75
REMARK 500 PRO A 152 -156.26 -81.39
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 NAP A1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LUM A1207
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HDO RELATED DB: PDB
REMARK 900 HUMAN BILIVERDIN IX BETA REDUCTASE: NADP COMPLEX
REMARK 900 RELATED ID: 1HE2 RELATED DB: PDB
REMARK 900 HUMAN BILIVERDIN IX BETA REDUCTASE: NADP/BILIVERDIN IX ALPHA
REMARK 900 TERNARY COMPLEX
REMARK 900 RELATED ID: 1HE3 RELATED DB: PDB
REMARK 900 HUMAN BILIVERDIN IX BETA REDUCTASE: NADP/MESOBILIVERDIN IV ALPHA
REMARK 900 TERNARY COMPLEX
REMARK 900 RELATED ID: 1HE4 RELATED DB: PDB
REMARK 900 HUMAN BILIVERDIN IX BETA REDUCTASE: NADP/FMN TERNARY COMPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PDB ENTRY CONTAINS AN EXTRA N-TERMINAL METHIONINE
DBREF 1HE5 A 1 1 PDB 1HE5 1HE5 1 1
DBREF 1HE5 A 2 205 UNP P30043 FLRE_HUMAN 1 204
SEQRES 1 A 206 MET ALA VAL LYS LYS ILE ALA ILE PHE GLY ALA THR GLY
SEQRES 2 A 206 GLN THR GLY LEU THR THR LEU ALA GLN ALA VAL GLN ALA
SEQRES 3 A 206 GLY TYR GLU VAL THR VAL LEU VAL ARG ASP SER SER ARG
SEQRES 4 A 206 LEU PRO SER GLU GLY PRO ARG PRO ALA HIS VAL VAL VAL
SEQRES 5 A 206 GLY ASP VAL LEU GLN ALA ALA ASP VAL ASP LYS THR VAL
SEQRES 6 A 206 ALA GLY GLN ASP ALA VAL ILE VAL LEU LEU GLY THR ARG
SEQRES 7 A 206 ASN ASP LEU SER PRO THR THR VAL MET SER GLU GLY ALA
SEQRES 8 A 206 ARG ASN ILE VAL ALA ALA MET LYS ALA HIS GLY VAL ASP
SEQRES 9 A 206 LYS VAL VAL ALA CYS THR SER ALA PHE LEU LEU TRP ASP
SEQRES 10 A 206 PRO THR LYS VAL PRO PRO ARG LEU GLN ALA VAL THR ASP
SEQRES 11 A 206 ASP HIS ILE ARG MET HIS LYS VAL LEU ARG GLU SER GLY
SEQRES 12 A 206 LEU LYS TYR VAL ALA VAL MET PRO PRO HIS ILE GLY ASP
SEQRES 13 A 206 GLN PRO LEU THR GLY ALA TYR THR VAL THR LEU ASP GLY
SEQRES 14 A 206 ARG GLY PRO SER ARG VAL ILE SER LYS HIS ASP LEU GLY
SEQRES 15 A 206 HIS PHE MET LEU ARG CYS LEU THR THR ASP GLU TYR ASP
SEQRES 16 A 206 GLY HIS SER THR TYR PRO SER HIS GLN TYR GLN
HET NAP A1206 48
HET LUM A1207 18
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM LUM LUMICHROME
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN LUM 7,8-DIMETHYLALLOXAZINE; 6,7-DIMETHYLALLOXAZINE
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 LUM C12 H10 N4 O2
FORMUL 4 HOH *271(H2 O)
HELIX 1 1 GLY A 13 GLY A 27 1 15
HELIX 2 2 ASP A 36 LEU A 40 5 5
HELIX 3 3 GLN A 57 ALA A 66 1 10
HELIX 4 4 THR A 85 GLY A 102 1 18
HELIX 5 5 SER A 111 LEU A 115 5 5
HELIX 6 6 PRO A 122 ARG A 124 5 3
HELIX 7 7 LEU A 125 GLU A 141 1 17
HELIX 8 8 LYS A 178 CYS A 188 1 11
SHEET 1 AA 8 HIS A 49 VAL A 52 0
SHEET 2 AA 8 GLU A 29 VAL A 34 1 O VAL A 30 N HIS A 49
SHEET 3 AA 8 LYS A 5 PHE A 9 1 O ILE A 6 N THR A 31
SHEET 4 AA 8 ALA A 70 VAL A 73 1 O ALA A 70 N ALA A 7
SHEET 5 AA 8 LYS A 105 CYS A 109 1 O LYS A 105 N VAL A 71
SHEET 6 AA 8 LYS A 145 VAL A 149 1 O LYS A 145 N VAL A 106
SHEET 7 AA 8 SER A 198 SER A 202 1 N THR A 199 O ALA A 148
SHEET 8 AA 8 THR A 164 THR A 166 -1 O THR A 164 N SER A 202
SHEET 1 AB 2 HIS A 153 GLY A 155 0
SHEET 2 AB 2 VAL A 175 SER A 177 1 O ILE A 176 N GLY A 155
SITE 1 AC1 34 GLY A 10 THR A 12 GLY A 13 GLN A 14
SITE 2 AC1 34 THR A 15 ARG A 35 ARG A 39 ASP A 54
SITE 3 AC1 34 VAL A 55 LEU A 74 LEU A 75 GLY A 76
SITE 4 AC1 34 ARG A 78 MET A 87 CYS A 109 THR A 110
SITE 5 AC1 34 SER A 111 HIS A 132 PRO A 151 PRO A 152
SITE 6 AC1 34 HIS A 153 ILE A 154 LUM A1207 HOH A2028
SITE 7 AC1 34 HOH A2065 HOH A2262 HOH A2263 HOH A2264
SITE 8 AC1 34 HOH A2265 HOH A2266 HOH A2267 HOH A2268
SITE 9 AC1 34 HOH A2269 HOH A2270
SITE 1 AC2 11 SER A 111 ALA A 112 PHE A 113 TRP A 116
SITE 2 AC2 11 VAL A 128 HIS A 132 PRO A 151 PRO A 152
SITE 3 AC2 11 HIS A 153 NAP A1206 HOH A2271
CRYST1 40.100 49.200 106.900 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 0.024938 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020325 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009354 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
