HEADER OXIDOREDUCTASE 13-AUG-04 1X7G
TITLE ACTINORHODIN POLYKETIDE KETOREDUCTASE, ACT KR, WITH NADP BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE KETOACYL REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACT KR, ACTINORHODIN POLYKETIDE KETOREDUCTASE;
COMPND 5 EC: 1.3.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;
SOURCE 3 ORGANISM_TAXID: 1902;
SOURCE 4 STRAIN: CH999;
SOURCE 5 GENE: ACTIII;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28C
KEYWDS POLYKETIDE, KETOREDUCTASE, SHORT CHAIN DEHYDROGENASE/REDUCTASE,
KEYWDS 2 COMBINATORIAL BIOSYNTHESIS, ACTINORHODIN, ANTIBIOTIC, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.P.KORMAN,J.A.HILL,T.N.VU
REVDAT 4 14-FEB-24 1X7G 1 REMARK
REVDAT 3 13-JUL-11 1X7G 1 VERSN
REVDAT 2 24-FEB-09 1X7G 1 VERSN
REVDAT 1 14-DEC-04 1X7G 0
JRNL AUTH T.P.KORMAN,J.A.HILL,T.N.VU,S.C.TSAI
JRNL TITL STRUCTURAL ANALYSIS OF ACTINORHODIN POLYKETIDE
JRNL TITL 2 KETOREDUCTASE: COFACTOR BINDING AND SUBSTRATE SPECIFICITY
JRNL REF BIOCHEMISTRY V. 43 14529 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15544323
JRNL DOI 10.1021/BI048133A
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 159974.900
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 33832
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) : 0.211
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1722
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4976
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 267
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3679
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 272
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.94000
REMARK 3 B22 (A**2) : 2.94000
REMARK 3 B33 (A**2) : -5.87000
REMARK 3 B12 (A**2) : 4.17000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.22
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) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.840
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 44.65
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NADP.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NADP.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030034.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
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 : 35529
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 26.60
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : 0.11500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.10
REMARK 200 R MERGE FOR SHELL (I) : 0.73400
REMARK 200 R SYM FOR SHELL (I) : 0.85700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
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 (%): 74.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.83333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.41667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 41.41667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 82.83333
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: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED
REMARK 300 BY THE TWO FOLD AXIS: X-Y, -Y, 1/3-Z
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 16630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -82.83333
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 ALA A 2
REMARK 465 THR A 3
REMARK 465 GLN A 4
REMARK 465 ASP A 5
REMARK 465 HIS B 201
REMARK 465 TYR B 202
REMARK 465 SER B 203
REMARK 465 ASP B 204
REMARK 465 ILE B 205
REMARK 465 TRP B 206
REMARK 465 GLU B 207
REMARK 465 VAL B 208
REMARK 465 SER B 209
REMARK 465 THR B 210
REMARK 465 GLU B 211
REMARK 465 GLU B 212
REMARK 465 ALA B 213
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 O ALA B 143 O HOH B 385 2.14
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 O ASN A 260 O HOH A 319 5554 2.19
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 LYS A 127 -86.97 -83.21
REMARK 500 ALA A 143 -119.41 -101.16
REMARK 500 SER A 144 164.80 178.10
REMARK 500 GLU A 191 89.57 -61.53
REMARK 500 ALA B 37 166.65 176.19
REMARK 500 LEU B 115 -65.12 -94.37
REMARK 500 LYS B 127 -88.94 -87.44
REMARK 500 ALA B 143 -119.17 -98.54
REMARK 500 SER B 144 169.29 174.01
REMARK 500 ALA B 154 48.76 -148.63
REMARK 500 ARG B 199 98.69 -58.31
REMARK 500 ASP B 215 10.35 -163.39
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 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X7H RELATED DB: PDB
DBREF 1X7G A 1 261 UNP P16544 ACT3_STRCO 1 261
DBREF 1X7G B 1 261 UNP P16544 ACT3_STRCO 1 261
SEQRES 1 A 261 MET ALA THR GLN ASP SER GLU VAL ALA LEU VAL THR GLY
SEQRES 2 A 261 ALA THR SER GLY ILE GLY LEU GLU ILE ALA ARG ARG LEU
SEQRES 3 A 261 GLY LYS GLU GLY LEU ARG VAL PHE VAL CYS ALA ARG GLY
SEQRES 4 A 261 GLU GLU GLY LEU ARG THR THR LEU LYS GLU LEU ARG GLU
SEQRES 5 A 261 ALA GLY VAL GLU ALA ASP GLY ARG THR CYS ASP VAL ARG
SEQRES 6 A 261 SER VAL PRO GLU ILE GLU ALA LEU VAL ALA ALA VAL VAL
SEQRES 7 A 261 GLU ARG TYR GLY PRO VAL ASP VAL LEU VAL ASN ASN ALA
SEQRES 8 A 261 GLY ARG PRO GLY GLY GLY ALA THR ALA GLU LEU ALA ASP
SEQRES 9 A 261 GLU LEU TRP LEU ASP VAL VAL GLU THR ASN LEU THR GLY
SEQRES 10 A 261 VAL PHE ARG VAL THR LYS GLN VAL LEU LYS ALA GLY GLY
SEQRES 11 A 261 MET LEU GLU ARG GLY THR GLY ARG ILE VAL ASN ILE ALA
SEQRES 12 A 261 SER THR GLY GLY LYS GLN GLY VAL VAL HIS ALA ALA PRO
SEQRES 13 A 261 TYR SER ALA SER LYS HIS GLY VAL VAL GLY PHE THR LYS
SEQRES 14 A 261 ALA LEU GLY LEU GLU LEU ALA ARG THR GLY ILE THR VAL
SEQRES 15 A 261 ASN ALA VAL CYS PRO GLY PHE VAL GLU THR PRO MET ALA
SEQRES 16 A 261 ALA SER VAL ARG GLU HIS TYR SER ASP ILE TRP GLU VAL
SEQRES 17 A 261 SER THR GLU GLU ALA PHE ASP ARG ILE THR ALA ARG VAL
SEQRES 18 A 261 PRO ILE GLY ARG TYR VAL GLN PRO SER GLU VAL ALA GLU
SEQRES 19 A 261 MET VAL ALA TYR LEU ILE GLY PRO GLY ALA ALA ALA VAL
SEQRES 20 A 261 THR ALA GLN ALA LEU ASN VAL CYS GLY GLY LEU GLY ASN
SEQRES 21 A 261 TYR
SEQRES 1 B 261 MET ALA THR GLN ASP SER GLU VAL ALA LEU VAL THR GLY
SEQRES 2 B 261 ALA THR SER GLY ILE GLY LEU GLU ILE ALA ARG ARG LEU
SEQRES 3 B 261 GLY LYS GLU GLY LEU ARG VAL PHE VAL CYS ALA ARG GLY
SEQRES 4 B 261 GLU GLU GLY LEU ARG THR THR LEU LYS GLU LEU ARG GLU
SEQRES 5 B 261 ALA GLY VAL GLU ALA ASP GLY ARG THR CYS ASP VAL ARG
SEQRES 6 B 261 SER VAL PRO GLU ILE GLU ALA LEU VAL ALA ALA VAL VAL
SEQRES 7 B 261 GLU ARG TYR GLY PRO VAL ASP VAL LEU VAL ASN ASN ALA
SEQRES 8 B 261 GLY ARG PRO GLY GLY GLY ALA THR ALA GLU LEU ALA ASP
SEQRES 9 B 261 GLU LEU TRP LEU ASP VAL VAL GLU THR ASN LEU THR GLY
SEQRES 10 B 261 VAL PHE ARG VAL THR LYS GLN VAL LEU LYS ALA GLY GLY
SEQRES 11 B 261 MET LEU GLU ARG GLY THR GLY ARG ILE VAL ASN ILE ALA
SEQRES 12 B 261 SER THR GLY GLY LYS GLN GLY VAL VAL HIS ALA ALA PRO
SEQRES 13 B 261 TYR SER ALA SER LYS HIS GLY VAL VAL GLY PHE THR LYS
SEQRES 14 B 261 ALA LEU GLY LEU GLU LEU ALA ARG THR GLY ILE THR VAL
SEQRES 15 B 261 ASN ALA VAL CYS PRO GLY PHE VAL GLU THR PRO MET ALA
SEQRES 16 B 261 ALA SER VAL ARG GLU HIS TYR SER ASP ILE TRP GLU VAL
SEQRES 17 B 261 SER THR GLU GLU ALA PHE ASP ARG ILE THR ALA ARG VAL
SEQRES 18 B 261 PRO ILE GLY ARG TYR VAL GLN PRO SER GLU VAL ALA GLU
SEQRES 19 B 261 MET VAL ALA TYR LEU ILE GLY PRO GLY ALA ALA ALA VAL
SEQRES 20 B 261 THR ALA GLN ALA LEU ASN VAL CYS GLY GLY LEU GLY ASN
SEQRES 21 B 261 TYR
HET NAP A 301 48
HET NAP B 301 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 5 HOH *272(H2 O)
HELIX 1 1 SER A 16 GLU A 29 1 14
HELIX 2 2 GLY A 39 GLU A 52 1 14
HELIX 3 3 SER A 66 TYR A 81 1 16
HELIX 4 4 ALA A 98 LEU A 102 5 5
HELIX 5 5 ALA A 103 LEU A 115 1 13
HELIX 6 6 LEU A 115 LYS A 127 1 13
HELIX 7 7 SER A 144 LYS A 148 5 5
HELIX 8 8 ALA A 154 LEU A 175 1 22
HELIX 9 9 THR A 192 TRP A 206 1 15
HELIX 10 10 SER A 209 ALA A 219 1 11
HELIX 11 11 GLN A 228 GLY A 241 1 14
HELIX 12 12 PRO A 242 ALA A 245 5 4
HELIX 13 13 SER B 16 LYS B 28 1 13
HELIX 14 14 GLY B 39 ALA B 53 1 15
HELIX 15 15 SER B 66 TYR B 81 1 16
HELIX 16 16 ALA B 98 LEU B 102 5 5
HELIX 17 17 ALA B 103 LEU B 115 1 13
HELIX 18 18 LEU B 115 LYS B 127 1 13
HELIX 19 19 GLY B 130 GLY B 135 1 6
HELIX 20 20 SER B 144 LYS B 148 5 5
HELIX 21 21 ALA B 154 LEU B 175 1 22
HELIX 22 22 THR B 192 ARG B 199 1 8
HELIX 23 23 GLN B 228 GLY B 241 1 14
HELIX 24 24 PRO B 242 ALA B 245 5 4
SHEET 1 A 7 ALA A 57 THR A 61 0
SHEET 2 A 7 ARG A 32 ALA A 37 1 N VAL A 35 O ARG A 60
SHEET 3 A 7 VAL A 8 VAL A 11 1 N ALA A 9 O PHE A 34
SHEET 4 A 7 VAL A 86 ASN A 89 1 O VAL A 88 N LEU A 10
SHEET 5 A 7 GLY A 137 ILE A 142 1 O VAL A 140 N LEU A 87
SHEET 6 A 7 ILE A 180 PRO A 187 1 O ASN A 183 N ASN A 141
SHEET 7 A 7 ALA A 251 VAL A 254 1 O LEU A 252 N CYS A 186
SHEET 1 B 7 ALA B 57 THR B 61 0
SHEET 2 B 7 ARG B 32 ALA B 37 1 N VAL B 35 O ASP B 58
SHEET 3 B 7 VAL B 8 VAL B 11 1 N ALA B 9 O ARG B 32
SHEET 4 B 7 VAL B 86 ASN B 89 1 O VAL B 88 N LEU B 10
SHEET 5 B 7 GLY B 137 ILE B 142 1 O VAL B 140 N LEU B 87
SHEET 6 B 7 ILE B 180 PRO B 187 1 O ASN B 183 N ASN B 141
SHEET 7 B 7 ALA B 251 VAL B 254 1 O LEU B 252 N CYS B 186
SITE 1 AC1 31 GLY A 13 THR A 15 SER A 16 GLY A 17
SITE 2 AC1 31 ILE A 18 ARG A 38 GLY A 39 CYS A 62
SITE 3 AC1 31 ASP A 63 VAL A 64 ASN A 90 GLY A 92
SITE 4 AC1 31 ILE A 142 ALA A 143 SER A 144 TYR A 157
SITE 5 AC1 31 LYS A 161 PRO A 187 GLY A 188 VAL A 190
SITE 6 AC1 31 THR A 192 PRO A 193 MET A 194 HOH A 302
SITE 7 AC1 31 HOH A 304 HOH A 314 HOH A 342 HOH A 359
SITE 8 AC1 31 HOH A 367 ARG B 51 HOH B 361
SITE 1 AC2 33 GLY B 13 THR B 15 SER B 16 GLY B 17
SITE 2 AC2 33 ILE B 18 ALA B 37 ARG B 38 GLY B 39
SITE 3 AC2 33 CYS B 62 ASP B 63 VAL B 64 ASN B 90
SITE 4 AC2 33 ALA B 91 GLY B 92 ILE B 142 ALA B 143
SITE 5 AC2 33 SER B 144 TYR B 157 LYS B 161 PRO B 187
SITE 6 AC2 33 GLY B 188 PHE B 189 VAL B 190 THR B 192
SITE 7 AC2 33 PRO B 193 MET B 194 HOH B 303 HOH B 385
SITE 8 AC2 33 HOH B 402 HOH B 423 HOH B 424 HOH B 425
SITE 9 AC2 33 HOH B 428
CRYST1 104.610 104.610 124.250 90.00 90.00 120.00 P 32 2 1 12
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 0.009559 0.005519 0.000000 0.00000
SCALE2 0.000000 0.011038 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008048 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
