HEADER OXIDOREDUCTASE 23-JAN-08 3C1O
TITLE THE MULTIPLE PHENYLPROPENE SYNTHASES IN BOTH CLARKIA BREWERI AND
TITLE 2 PETUNIA HYBRIDA REPRESENT TWO DISTINCT LINEAGES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUGENOL SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BREWER'S CLARKIA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLARKIA BREWERI;
SOURCE 3 ORGANISM_TAXID: 36903;
SOURCE 4 GENE: EGS1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHIS8
KEYWDS EUGENOL, PHENYLPROPENE, PIP REDUCTASE, SHORT-CHAIN
KEYWDS 2 DEHYDROGENASE/REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.V.LOUIE,J.P.NOEL,M.E.BOWMAN
REVDAT 3 21-FEB-24 3C1O 1 REMARK
REVDAT 2 24-FEB-09 3C1O 1 VERSN
REVDAT 1 06-MAY-08 3C1O 0
JRNL AUTH T.KOEDUKA,G.V.LOUIE,I.ORLOVA,C.M.KISH,M.IBDAH,C.G.WILKERSON,
JRNL AUTH 2 M.E.BOWMAN,T.J.BAIGA,J.P.NOEL,N.DUDAREVA,E.PICHERSKY
JRNL TITL THE MULTIPLE PHENYLPROPENE SYNTHASES IN BOTH CLARKIA BREWERI
JRNL TITL 2 AND PETUNIA HYBRIDA REPRESENT TWO DISTINCT PROTEIN LINEAGES.
JRNL REF PLANT J. V. 54 362 2008
JRNL REFN ISSN 0960-7412
JRNL PMID 18208524
JRNL DOI 10.1111/J.1365-313X.2008.03412.X
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) : 33.90
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) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 26856
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) : 0.186
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1347
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 : 2500
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.65100
REMARK 3 B22 (A**2) : -0.56300
REMARK 3 B33 (A**2) : 3.21300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.330
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.786 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.650 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.938 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.434 ; 4.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 45.89
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NDP.PAR
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3C1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000046229.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26859
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.434
REMARK 200 RESOLUTION RANGE LOW (A) : 50.572
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
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 (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.40100
REMARK 200 R SYM FOR SHELL (I) : 0.40100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, 20% (W/V) PEG
REMARK 280 4000, 20% (V/V) ISOPROPANOL, 2 MM DITHIOTHREITOL, 5 MM NADP+, PH
REMARK 280 5.4, VAPOR DIFFUSION, HANGING 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 33.66500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.69050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.66500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.69050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4650 ANGSTROM**2
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 124.53349
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 50.54049
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 A1201 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 ALA A 315
REMARK 465 GLU A 316
REMARK 465 PHE A 317
REMARK 465 GLU A 318
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 CD2 LEU A 314 CD2 LEU A 314 2756 2.08
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 110 -88.17 -101.74
REMARK 500 ASN A 151 -163.69 65.17
REMARK 500 HIS A 163 63.77 33.09
REMARK 500 ASP A 173 119.84 0.35
REMARK 500 MET A 274 10.37 -144.67
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 A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C3X RELATED DB: PDB
DBREF 3C1O A -2 318 PDB 3C1O 3C1O -2 318
SEQRES 1 A 321 GLY SER HIS MET GLU LYS ILE ILE ILE TYR GLY GLY THR
SEQRES 2 A 321 GLY TYR ILE GLY LYS PHE MET VAL ARG ALA SER LEU SER
SEQRES 3 A 321 PHE SER HIS PRO THR PHE ILE TYR ALA ARG PRO LEU THR
SEQRES 4 A 321 PRO ASP SER THR PRO SER SER VAL GLN LEU ARG GLU GLU
SEQRES 5 A 321 PHE ARG SER MET GLY VAL THR ILE ILE GLU GLY GLU MET
SEQRES 6 A 321 GLU GLU HIS GLU LYS MET VAL SER VAL LEU LYS GLN VAL
SEQRES 7 A 321 ASP ILE VAL ILE SER ALA LEU PRO PHE PRO MET ILE SER
SEQRES 8 A 321 SER GLN ILE HIS ILE ILE ASN ALA ILE LYS ALA ALA GLY
SEQRES 9 A 321 ASN ILE LYS ARG PHE LEU PRO SER ASP PHE GLY CYS GLU
SEQRES 10 A 321 GLU ASP ARG ILE LYS PRO LEU PRO PRO PHE GLU SER VAL
SEQRES 11 A 321 LEU GLU LYS LYS ARG ILE ILE ARG ARG ALA ILE GLU ALA
SEQRES 12 A 321 ALA ALA LEU PRO TYR THR TYR VAL SER ALA ASN CYS PHE
SEQRES 13 A 321 GLY ALA TYR PHE VAL ASN TYR LEU LEU HIS PRO SER PRO
SEQRES 14 A 321 HIS PRO ASN ARG ASN ASP ASP ILE VAL ILE TYR GLY THR
SEQRES 15 A 321 GLY GLU THR LYS PHE VAL LEU ASN TYR GLU GLU ASP ILE
SEQRES 16 A 321 ALA LYS TYR THR ILE LYS VAL ALA CYS ASP PRO ARG CYS
SEQRES 17 A 321 CYS ASN ARG ILE VAL ILE TYR ARG PRO PRO LYS ASN ILE
SEQRES 18 A 321 ILE SER GLN ASN GLU LEU ILE SER LEU TRP GLU ALA LYS
SEQRES 19 A 321 SER GLY LEU SER PHE LYS LYS VAL HIS MET PRO ASP GLU
SEQRES 20 A 321 GLN LEU VAL ARG LEU SER GLN GLU LEU PRO GLN PRO GLN
SEQRES 21 A 321 ASN ILE PRO VAL SER ILE LEU HIS SER ILE PHE VAL LYS
SEQRES 22 A 321 GLY ASP LEU MET SER TYR GLU MET ARG LYS ASP ASP ILE
SEQRES 23 A 321 GLU ALA SER ASN LEU TYR PRO GLU LEU GLU PHE THR SER
SEQRES 24 A 321 ILE ASP GLY LEU LEU ASP LEU PHE ILE SER GLY ARG ALA
SEQRES 25 A 321 PRO PRO PRO THR LEU ALA GLU PHE GLU
HET NAP A 401 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 HOH *210(H2 O)
HELIX 1 1 ILE A 13 PHE A 24 1 12
HELIX 2 2 THR A 40 MET A 53 1 14
HELIX 3 3 GLU A 64 LYS A 73 1 10
HELIX 4 4 PRO A 83 SER A 89 5 7
HELIX 5 5 GLN A 90 GLY A 101 1 12
HELIX 6 6 GLU A 114 ILE A 118 5 5
HELIX 7 7 LEU A 121 ALA A 142 1 22
HELIX 8 8 GLY A 154 HIS A 163 1 10
HELIX 9 9 TYR A 188 ASP A 202 1 15
HELIX 10 10 PRO A 203 CYS A 206 5 4
HELIX 11 11 PRO A 214 LYS A 216 5 3
HELIX 12 12 GLN A 221 GLY A 233 1 13
HELIX 13 13 PRO A 242 LEU A 253 1 12
HELIX 14 14 GLN A 257 VAL A 269 1 13
HELIX 15 15 SER A 286 LEU A 288 5 3
HELIX 16 16 SER A 296 SER A 306 1 11
SHEET 1 A 5 THR A 56 GLU A 59 0
SHEET 2 A 5 THR A 28 ALA A 32 1 N ILE A 30 O ILE A 58
SHEET 3 A 5 ILE A 4 TYR A 7 1 N ILE A 4 O PHE A 29
SHEET 4 A 5 ILE A 77 SER A 80 1 O ILE A 77 N ILE A 5
SHEET 5 A 5 ARG A 105 LEU A 107 1 O LEU A 107 N SER A 80
SHEET 1 B 3 THR A 146 SER A 149 0
SHEET 2 B 3 ARG A 208 ILE A 211 1 O VAL A 210 N SER A 149
SHEET 3 B 3 ILE A 283 GLU A 284 1 O ILE A 283 N ILE A 211
SHEET 1 C 3 CYS A 152 PHE A 153 0
SHEET 2 C 3 LYS A 183 ASN A 187 1 O ASN A 187 N CYS A 152
SHEET 3 C 3 ILE A 218 SER A 220 -1 O ILE A 219 N PHE A 184
SHEET 1 D 2 ILE A 174 TYR A 177 0
SHEET 2 D 2 LYS A 238 MET A 241 1 O VAL A 239 N ILE A 176
CISPEP 1 GLN A 255 PRO A 256 0 0.07
SITE 1 AC1 29 GLY A 8 THR A 10 GLY A 11 TYR A 12
SITE 2 AC1 29 ILE A 13 ARG A 33 SER A 43 ARG A 47
SITE 3 AC1 29 ALA A 81 LEU A 82 PRO A 83 PHE A 84
SITE 4 AC1 29 MET A 86 SER A 109 ASP A 110 PHE A 111
SITE 5 AC1 29 LYS A 131 ASN A 151 CYS A 152 PHE A 153
SITE 6 AC1 29 PHE A 157 HOH A1001 HOH A1055 HOH A1063
SITE 7 AC1 29 HOH A1083 HOH A1088 HOH A1106 HOH A1137
SITE 8 AC1 29 HOH A1146
CRYST1 67.330 87.381 51.545 90.00 101.33 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 0.014852 0.000000 0.002976 0.00000
SCALE2 0.000000 0.011444 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019786 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
