HEADER TRANSFERASE 26-MAR-04 1SUW
TITLE CRYSTAL STRUCTURE OF A NAD KINASE FROM ARCHAEOGLOBUS FULGIDUS IN
TITLE 2 COMPLEX WITH ITS SUBSTRATE AND PRODUCT: INSIGHTS INTO THE CATALYSIS
TITLE 3 OF NAD KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE INORGANIC POLYPHOSPHATE/ATP-NAD KINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: POLY(P)/ATP NAD KINASE;
COMPND 5 EC: 2.7.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 2234;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PSJS1244 STAR;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PB4
KEYWDS ATP-NAD KINASE, NADK, NAD, NADP, STRUCTURAL GENOMICS, BSGC STRUCTURE
KEYWDS 2 FUNDED BY NIH, PROTEIN STRUCTURE INITIATIVE, PSI, BERKELEY
KEYWDS 3 STRUCTURAL GENOMICS CENTER, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LIU,Y.LOU,H.YOKOTA,P.D.ADAMS,R.KIM,S.-H.KIM,BERKELEY STRUCTURAL
AUTHOR 2 GENOMICS CENTER (BSGC)
REVDAT 7 14-FEB-24 1SUW 1 REMARK
REVDAT 6 11-OCT-17 1SUW 1 REMARK
REVDAT 5 24-FEB-09 1SUW 1 VERSN
REVDAT 4 07-MAR-06 1SUW 1 JRNL
REVDAT 3 25-JAN-05 1SUW 1 AUTHOR KEYWDS REMARK
REVDAT 2 11-JAN-05 1SUW 1 AUTHOR JRNL TITLE
REVDAT 1 24-AUG-04 1SUW 0
JRNL AUTH J.LIU,Y.LOU,H.YOKOTA,P.D.ADAMS,R.KIM,S.-H.KIM
JRNL TITL CRYSTAL STRUCTURES OF AN NAD KINASE FROM ARCHAEOGLOBUS
JRNL TITL 2 FULGIDUS IN COMPLEX WITH ATP, NAD, OR NADP
JRNL REF J.MOL.BIOL. V. 354 289 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16242716
JRNL DOI 10.1016/J.JMB.2005.09.026
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 82.5
REMARK 3 NUMBER OF REFLECTIONS : 46127
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : 5%
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2342
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 : 7856
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 303
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) : -4.38000
REMARK 3 B22 (A**2) : -4.38000
REMARK 3 B33 (A**2) : 8.76000
REMARK 3 B12 (A**2) : 0.00000
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) : 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) : 0.008
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SUW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022010.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-DEC-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796, 0.9798, 0.9600
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62750
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
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) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM HEPES, 2M NACL, 10% PEG 6000, PH
REMARK 280 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 99.29750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 61.07050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 61.07050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 49.64875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 61.07050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 61.07050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 148.94625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 61.07050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.07050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 49.64875
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 61.07050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.07050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 148.94625
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 99.29750
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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: 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 GLY C 71 N - CA - C ANGL. DEV. = 29.2 DEGREES
REMARK 500 ARG C 72 N - CA - CB ANGL. DEV. = -18.0 DEGREES
REMARK 500 PRO C 109 C - N - CA ANGL. DEV. = 9.6 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 22 3.67 -61.40
REMARK 500 LYS A 60 -64.72 -91.80
REMARK 500 ASN A 83 34.08 -145.80
REMARK 500 PRO A 109 -37.53 -39.69
REMARK 500 ASP A 209 26.51 44.09
REMARK 500 ASP B 10 4.74 -68.81
REMARK 500 ASN B 39 35.22 -90.42
REMARK 500 LYS B 60 -70.28 -88.28
REMARK 500 ASN B 83 19.22 -150.44
REMARK 500 GLU B 85 -70.49 -53.87
REMARK 500 ASP B 140 147.46 -171.67
REMARK 500 ASP B 209 24.93 47.95
REMARK 500 GLU C 18 0.80 -63.77
REMARK 500 LYS C 60 -68.00 -97.65
REMARK 500 ARG C 72 -80.85 -117.87
REMARK 500 ASN C 83 28.97 -163.11
REMARK 500 ASP C 209 22.66 44.62
REMARK 500 VAL C 214 138.12 -179.02
REMARK 500 ASN D 39 35.38 -87.46
REMARK 500 ARG D 72 -72.15 -88.19
REMARK 500 ASN D 83 15.25 -146.02
REMARK 500 ALA D 125 16.23 58.46
REMARK 500 ASP D 140 155.94 172.74
REMARK 500 GLN D 211 -73.85 -99.02
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 3075
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 3076
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 3077
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 3078
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BSGCAIR30424 RELATED DB: TARGETDB
DBREF 1SUW A 1 249 UNP O30297 PPNK_ARCFU 1 249
DBREF 1SUW B 1 249 UNP O30297 PPNK_ARCFU 1 249
DBREF 1SUW C 1 249 UNP O30297 PPNK_ARCFU 1 249
DBREF 1SUW D 1 249 UNP O30297 PPNK_ARCFU 1 249
SEQRES 1 A 249 MET ARG ALA ALA VAL VAL TYR LYS THR ASP GLY HIS VAL
SEQRES 2 A 249 LYS ARG ILE GLU GLU ALA LEU LYS ARG LEU GLU VAL GLU
SEQRES 3 A 249 VAL GLU LEU PHE ASN GLN PRO SER GLU GLU LEU GLU ASN
SEQRES 4 A 249 PHE ASP PHE ILE VAL SER VAL GLY GLY ASP GLY THR ILE
SEQRES 5 A 249 LEU ARG ILE LEU GLN LYS LEU LYS ARG CYS PRO PRO ILE
SEQRES 6 A 249 PHE GLY ILE ASN THR GLY ARG VAL GLY LEU LEU THR HIS
SEQRES 7 A 249 ALA SER PRO GLU ASN PHE GLU VAL GLU LEU LYS LYS ALA
SEQRES 8 A 249 VAL GLU LYS PHE GLU VAL GLU ARG PHE PRO ARG VAL SER
SEQRES 9 A 249 CYS SER ALA MET PRO ASP VAL LEU ALA LEU ASN GLU ILE
SEQRES 10 A 249 ALA VAL LEU SER ARG LYS PRO ALA LYS MET ILE ASP VAL
SEQRES 11 A 249 ALA LEU ARG VAL ASP GLY VAL GLU VAL ASP ARG ILE ARG
SEQRES 12 A 249 CYS ASP GLY PHE ILE VAL ALA THR GLN ILE GLY SER THR
SEQRES 13 A 249 GLY TYR ALA PHE SER ALA GLY GLY PRO VAL VAL GLU PRO
SEQRES 14 A 249 TYR LEU GLU CYS PHE ILE LEU ILE PRO ILE ALA PRO PHE
SEQRES 15 A 249 ARG PHE GLY TRP LYS PRO TYR VAL VAL SER MET GLU ARG
SEQRES 16 A 249 LYS ILE GLU VAL ILE ALA GLU LYS ALA ILE VAL VAL ALA
SEQRES 17 A 249 ASP GLY GLN LYS SER VAL ASP PHE ASP GLY GLU ILE THR
SEQRES 18 A 249 ILE GLU LYS SER GLU PHE PRO ALA VAL PHE PHE LYS ASN
SEQRES 19 A 249 GLU LYS ARG PHE ARG ASN LEU PHE GLY LYS VAL ARG SER
SEQRES 20 A 249 ILE GLY
SEQRES 1 B 249 MET ARG ALA ALA VAL VAL TYR LYS THR ASP GLY HIS VAL
SEQRES 2 B 249 LYS ARG ILE GLU GLU ALA LEU LYS ARG LEU GLU VAL GLU
SEQRES 3 B 249 VAL GLU LEU PHE ASN GLN PRO SER GLU GLU LEU GLU ASN
SEQRES 4 B 249 PHE ASP PHE ILE VAL SER VAL GLY GLY ASP GLY THR ILE
SEQRES 5 B 249 LEU ARG ILE LEU GLN LYS LEU LYS ARG CYS PRO PRO ILE
SEQRES 6 B 249 PHE GLY ILE ASN THR GLY ARG VAL GLY LEU LEU THR HIS
SEQRES 7 B 249 ALA SER PRO GLU ASN PHE GLU VAL GLU LEU LYS LYS ALA
SEQRES 8 B 249 VAL GLU LYS PHE GLU VAL GLU ARG PHE PRO ARG VAL SER
SEQRES 9 B 249 CYS SER ALA MET PRO ASP VAL LEU ALA LEU ASN GLU ILE
SEQRES 10 B 249 ALA VAL LEU SER ARG LYS PRO ALA LYS MET ILE ASP VAL
SEQRES 11 B 249 ALA LEU ARG VAL ASP GLY VAL GLU VAL ASP ARG ILE ARG
SEQRES 12 B 249 CYS ASP GLY PHE ILE VAL ALA THR GLN ILE GLY SER THR
SEQRES 13 B 249 GLY TYR ALA PHE SER ALA GLY GLY PRO VAL VAL GLU PRO
SEQRES 14 B 249 TYR LEU GLU CYS PHE ILE LEU ILE PRO ILE ALA PRO PHE
SEQRES 15 B 249 ARG PHE GLY TRP LYS PRO TYR VAL VAL SER MET GLU ARG
SEQRES 16 B 249 LYS ILE GLU VAL ILE ALA GLU LYS ALA ILE VAL VAL ALA
SEQRES 17 B 249 ASP GLY GLN LYS SER VAL ASP PHE ASP GLY GLU ILE THR
SEQRES 18 B 249 ILE GLU LYS SER GLU PHE PRO ALA VAL PHE PHE LYS ASN
SEQRES 19 B 249 GLU LYS ARG PHE ARG ASN LEU PHE GLY LYS VAL ARG SER
SEQRES 20 B 249 ILE GLY
SEQRES 1 C 249 MET ARG ALA ALA VAL VAL TYR LYS THR ASP GLY HIS VAL
SEQRES 2 C 249 LYS ARG ILE GLU GLU ALA LEU LYS ARG LEU GLU VAL GLU
SEQRES 3 C 249 VAL GLU LEU PHE ASN GLN PRO SER GLU GLU LEU GLU ASN
SEQRES 4 C 249 PHE ASP PHE ILE VAL SER VAL GLY GLY ASP GLY THR ILE
SEQRES 5 C 249 LEU ARG ILE LEU GLN LYS LEU LYS ARG CYS PRO PRO ILE
SEQRES 6 C 249 PHE GLY ILE ASN THR GLY ARG VAL GLY LEU LEU THR HIS
SEQRES 7 C 249 ALA SER PRO GLU ASN PHE GLU VAL GLU LEU LYS LYS ALA
SEQRES 8 C 249 VAL GLU LYS PHE GLU VAL GLU ARG PHE PRO ARG VAL SER
SEQRES 9 C 249 CYS SER ALA MET PRO ASP VAL LEU ALA LEU ASN GLU ILE
SEQRES 10 C 249 ALA VAL LEU SER ARG LYS PRO ALA LYS MET ILE ASP VAL
SEQRES 11 C 249 ALA LEU ARG VAL ASP GLY VAL GLU VAL ASP ARG ILE ARG
SEQRES 12 C 249 CYS ASP GLY PHE ILE VAL ALA THR GLN ILE GLY SER THR
SEQRES 13 C 249 GLY TYR ALA PHE SER ALA GLY GLY PRO VAL VAL GLU PRO
SEQRES 14 C 249 TYR LEU GLU CYS PHE ILE LEU ILE PRO ILE ALA PRO PHE
SEQRES 15 C 249 ARG PHE GLY TRP LYS PRO TYR VAL VAL SER MET GLU ARG
SEQRES 16 C 249 LYS ILE GLU VAL ILE ALA GLU LYS ALA ILE VAL VAL ALA
SEQRES 17 C 249 ASP GLY GLN LYS SER VAL ASP PHE ASP GLY GLU ILE THR
SEQRES 18 C 249 ILE GLU LYS SER GLU PHE PRO ALA VAL PHE PHE LYS ASN
SEQRES 19 C 249 GLU LYS ARG PHE ARG ASN LEU PHE GLY LYS VAL ARG SER
SEQRES 20 C 249 ILE GLY
SEQRES 1 D 249 MET ARG ALA ALA VAL VAL TYR LYS THR ASP GLY HIS VAL
SEQRES 2 D 249 LYS ARG ILE GLU GLU ALA LEU LYS ARG LEU GLU VAL GLU
SEQRES 3 D 249 VAL GLU LEU PHE ASN GLN PRO SER GLU GLU LEU GLU ASN
SEQRES 4 D 249 PHE ASP PHE ILE VAL SER VAL GLY GLY ASP GLY THR ILE
SEQRES 5 D 249 LEU ARG ILE LEU GLN LYS LEU LYS ARG CYS PRO PRO ILE
SEQRES 6 D 249 PHE GLY ILE ASN THR GLY ARG VAL GLY LEU LEU THR HIS
SEQRES 7 D 249 ALA SER PRO GLU ASN PHE GLU VAL GLU LEU LYS LYS ALA
SEQRES 8 D 249 VAL GLU LYS PHE GLU VAL GLU ARG PHE PRO ARG VAL SER
SEQRES 9 D 249 CYS SER ALA MET PRO ASP VAL LEU ALA LEU ASN GLU ILE
SEQRES 10 D 249 ALA VAL LEU SER ARG LYS PRO ALA LYS MET ILE ASP VAL
SEQRES 11 D 249 ALA LEU ARG VAL ASP GLY VAL GLU VAL ASP ARG ILE ARG
SEQRES 12 D 249 CYS ASP GLY PHE ILE VAL ALA THR GLN ILE GLY SER THR
SEQRES 13 D 249 GLY TYR ALA PHE SER ALA GLY GLY PRO VAL VAL GLU PRO
SEQRES 14 D 249 TYR LEU GLU CYS PHE ILE LEU ILE PRO ILE ALA PRO PHE
SEQRES 15 D 249 ARG PHE GLY TRP LYS PRO TYR VAL VAL SER MET GLU ARG
SEQRES 16 D 249 LYS ILE GLU VAL ILE ALA GLU LYS ALA ILE VAL VAL ALA
SEQRES 17 D 249 ASP GLY GLN LYS SER VAL ASP PHE ASP GLY GLU ILE THR
SEQRES 18 D 249 ILE GLU LYS SER GLU PHE PRO ALA VAL PHE PHE LYS ASN
SEQRES 19 D 249 GLU LYS ARG PHE ARG ASN LEU PHE GLY LYS VAL ARG SER
SEQRES 20 D 249 ILE GLY
HET NAP A3075 48
HET NAP B3076 48
HET NAP C3077 48
HET NAP D3078 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 5 NAP 4(C21 H28 N7 O17 P3)
FORMUL 9 HOH *303(H2 O)
HELIX 1 1 HIS A 12 ARG A 22 1 11
HELIX 2 2 SER A 34 PHE A 40 5 7
HELIX 3 3 GLY A 48 GLN A 57 1 10
HELIX 4 4 SER A 80 GLU A 82 5 3
HELIX 5 5 ASN A 83 PHE A 95 1 13
HELIX 6 6 ILE A 153 THR A 156 5 4
HELIX 7 7 GLY A 157 ALA A 162 1 6
HELIX 8 8 LYS A 236 ARG A 246 1 11
HELIX 9 9 HIS B 12 LEU B 23 1 12
HELIX 10 10 SER B 34 PHE B 40 5 7
HELIX 11 11 GLY B 48 GLN B 57 1 10
HELIX 12 12 ASN B 83 PHE B 95 1 13
HELIX 13 13 ILE B 153 THR B 156 5 4
HELIX 14 14 GLY B 157 ALA B 162 1 6
HELIX 15 15 LYS B 236 SER B 247 1 12
HELIX 16 16 HIS C 12 LYS C 21 1 10
HELIX 17 17 SER C 34 PHE C 40 5 7
HELIX 18 18 GLY C 48 GLN C 57 1 10
HELIX 19 19 ASN C 83 PHE C 95 1 13
HELIX 20 20 ILE C 153 THR C 156 5 4
HELIX 21 21 GLY C 157 ALA C 162 1 6
HELIX 22 22 LYS C 236 SER C 247 1 12
HELIX 23 23 HIS D 12 LEU D 23 1 12
HELIX 24 24 SER D 34 PHE D 40 5 7
HELIX 25 25 GLY D 48 GLN D 57 1 10
HELIX 26 26 ASN D 83 PHE D 95 1 13
HELIX 27 27 ILE D 153 THR D 156 5 4
HELIX 28 28 GLY D 157 ALA D 162 1 6
HELIX 29 29 LYS D 236 SER D 247 1 12
SHEET 1 A 4 GLU A 26 PHE A 30 0
SHEET 2 A 4 ARG A 2 TYR A 7 1 N ALA A 3 O GLU A 26
SHEET 3 A 4 PHE A 42 GLY A 47 1 O VAL A 44 N ALA A 4
SHEET 4 A 4 ILE A 65 ASN A 69 1 O PHE A 66 N SER A 45
SHEET 1 B 2 VAL A 97 PHE A 100 0
SHEET 2 B 2 ALA A 229 PHE A 232 -1 O ALA A 229 N PHE A 100
SHEET 1 C 5 VAL A 103 CYS A 105 0
SHEET 2 C 5 LYS A 212 LYS A 224 -1 O GLU A 223 N SER A 104
SHEET 3 C 5 ILE A 197 ALA A 208 -1 N ILE A 197 O ILE A 222
SHEET 4 C 5 ILE A 128 VAL A 134 -1 N ARG A 133 O GLU A 198
SHEET 5 C 5 VAL A 137 CYS A 144 -1 O ASP A 140 N LEU A 132
SHEET 1 D 8 VAL A 103 CYS A 105 0
SHEET 2 D 8 LYS A 212 LYS A 224 -1 O GLU A 223 N SER A 104
SHEET 3 D 8 ILE A 197 ALA A 208 -1 N ILE A 197 O ILE A 222
SHEET 4 D 8 GLU A 116 SER A 121 -1 N ALA A 118 O VAL A 207
SHEET 5 D 8 GLY A 146 THR A 151 -1 O PHE A 147 N VAL A 119
SHEET 6 D 8 PHE A 174 ILE A 179 -1 O ILE A 177 N ILE A 148
SHEET 7 D 8 TYR A 189 VAL A 191 -1 O VAL A 191 N PHE A 174
SHEET 8 D 8 VAL B 166 VAL B 167 1 O VAL B 166 N VAL A 190
SHEET 1 E 9 VAL A 166 VAL A 167 0
SHEET 2 E 9 TYR B 189 SER B 192 1 O VAL B 190 N VAL A 166
SHEET 3 E 9 CYS B 173 ILE B 179 -1 N PHE B 174 O VAL B 191
SHEET 4 E 9 GLY B 146 THR B 151 -1 N ILE B 148 O ILE B 177
SHEET 5 E 9 GLU B 116 SER B 121 -1 N VAL B 119 O PHE B 147
SHEET 6 E 9 ILE B 197 ALA B 208 -1 O VAL B 207 N ALA B 118
SHEET 7 E 9 LYS B 212 LYS B 224 -1 O ILE B 222 N ILE B 197
SHEET 8 E 9 VAL B 103 CYS B 105 -1 N SER B 104 O GLU B 223
SHEET 9 E 9 MET B 108 ALA B 113 -1 O ALA B 113 N VAL B 103
SHEET 1 F 8 VAL A 166 VAL A 167 0
SHEET 2 F 8 TYR B 189 SER B 192 1 O VAL B 190 N VAL A 166
SHEET 3 F 8 CYS B 173 ILE B 179 -1 N PHE B 174 O VAL B 191
SHEET 4 F 8 GLY B 146 THR B 151 -1 N ILE B 148 O ILE B 177
SHEET 5 F 8 GLU B 116 SER B 121 -1 N VAL B 119 O PHE B 147
SHEET 6 F 8 ILE B 197 ALA B 208 -1 O VAL B 207 N ALA B 118
SHEET 7 F 8 ILE B 128 VAL B 134 -1 N ARG B 133 O GLU B 198
SHEET 8 F 8 VAL B 137 CYS B 144 -1 O ILE B 142 N VAL B 130
SHEET 1 G 4 GLU B 26 PHE B 30 0
SHEET 2 G 4 ARG B 2 TYR B 7 1 N ALA B 3 O GLU B 26
SHEET 3 G 4 PHE B 42 GLY B 47 1 O VAL B 44 N ALA B 4
SHEET 4 G 4 ILE B 65 ASN B 69 1 O ILE B 68 N GLY B 47
SHEET 1 H 2 VAL B 97 PHE B 100 0
SHEET 2 H 2 ALA B 229 PHE B 232 -1 O PHE B 231 N GLU B 98
SHEET 1 I 4 GLU C 26 PHE C 30 0
SHEET 2 I 4 ARG C 2 TYR C 7 1 N VAL C 5 O GLU C 28
SHEET 3 I 4 PHE C 42 GLY C 47 1 O VAL C 44 N ALA C 4
SHEET 4 I 4 ILE C 65 ASN C 69 1 O ILE C 68 N SER C 45
SHEET 1 J 2 VAL C 97 PHE C 100 0
SHEET 2 J 2 ALA C 229 PHE C 232 -1 O ALA C 229 N PHE C 100
SHEET 1 K 5 VAL C 103 CYS C 105 0
SHEET 2 K 5 LYS C 212 LYS C 224 -1 O GLU C 223 N SER C 104
SHEET 3 K 5 ILE C 197 ALA C 208 -1 N ILE C 197 O ILE C 222
SHEET 4 K 5 ILE C 128 VAL C 134 -1 N ARG C 133 O GLU C 198
SHEET 5 K 5 VAL C 137 CYS C 144 -1 O ASP C 140 N LEU C 132
SHEET 1 L 8 VAL C 103 CYS C 105 0
SHEET 2 L 8 LYS C 212 LYS C 224 -1 O GLU C 223 N SER C 104
SHEET 3 L 8 ILE C 197 ALA C 208 -1 N ILE C 197 O ILE C 222
SHEET 4 L 8 GLU C 116 SER C 121 -1 N ALA C 118 O VAL C 207
SHEET 5 L 8 GLY C 146 THR C 151 -1 O PHE C 147 N VAL C 119
SHEET 6 L 8 PHE C 174 ILE C 179 -1 O ILE C 177 N ILE C 148
SHEET 7 L 8 TYR C 189 VAL C 191 -1 O TYR C 189 N LEU C 176
SHEET 8 L 8 VAL D 166 VAL D 167 1 O VAL D 166 N VAL C 190
SHEET 1 M 9 VAL C 166 VAL C 167 0
SHEET 2 M 9 TYR D 189 VAL D 191 1 O VAL D 190 N VAL C 166
SHEET 3 M 9 PHE D 174 ILE D 179 -1 N PHE D 174 O VAL D 191
SHEET 4 M 9 GLY D 146 ALA D 150 -1 N ILE D 148 O ILE D 177
SHEET 5 M 9 GLU D 116 SER D 121 -1 N VAL D 119 O PHE D 147
SHEET 6 M 9 ILE D 197 ALA D 208 -1 O VAL D 207 N ALA D 118
SHEET 7 M 9 LYS D 212 LYS D 224 -1 O ILE D 222 N ILE D 197
SHEET 8 M 9 VAL D 103 CYS D 105 -1 N SER D 104 O GLU D 223
SHEET 9 M 9 MET D 108 ALA D 113 -1 O ALA D 113 N VAL D 103
SHEET 1 N 8 VAL C 166 VAL C 167 0
SHEET 2 N 8 TYR D 189 VAL D 191 1 O VAL D 190 N VAL C 166
SHEET 3 N 8 PHE D 174 ILE D 179 -1 N PHE D 174 O VAL D 191
SHEET 4 N 8 GLY D 146 ALA D 150 -1 N ILE D 148 O ILE D 177
SHEET 5 N 8 GLU D 116 SER D 121 -1 N VAL D 119 O PHE D 147
SHEET 6 N 8 ILE D 197 ALA D 208 -1 O VAL D 207 N ALA D 118
SHEET 7 N 8 ILE D 128 VAL D 134 -1 N ARG D 133 O GLU D 198
SHEET 8 N 8 VAL D 137 CYS D 144 -1 O ASP D 140 N LEU D 132
SHEET 1 O 4 GLU D 26 PHE D 30 0
SHEET 2 O 4 ARG D 2 TYR D 7 1 N ALA D 3 O GLU D 26
SHEET 3 O 4 PHE D 42 GLY D 47 1 O VAL D 44 N ALA D 4
SHEET 4 O 4 ILE D 65 ASN D 69 1 O PHE D 66 N ILE D 43
SHEET 1 P 2 VAL D 97 PHE D 100 0
SHEET 2 P 2 ALA D 229 PHE D 232 -1 O PHE D 231 N GLU D 98
SITE 1 AC1 23 GLY A 48 ASP A 49 GLY A 50 ARG A 54
SITE 2 AC1 23 VAL A 73 ASN A 115 GLU A 116 ILE A 153
SITE 3 AC1 23 THR A 156 GLY A 157 TYR A 158 SER A 161
SITE 4 AC1 23 ASP A 209 GLY A 210 GLN A 211 HOH A3082
SITE 5 AC1 23 ALA D 125 LYS D 126 MET D 127 ARG D 143
SITE 6 AC1 23 ASP D 145 ALA D 180 PHE D 182
SITE 1 AC2 25 GLY B 48 ASP B 49 GLY B 50 LEU B 53
SITE 2 AC2 25 ARG B 54 VAL B 73 LEU B 75 ASN B 115
SITE 3 AC2 25 GLU B 116 ILE B 153 THR B 156 TYR B 158
SITE 4 AC2 25 SER B 161 ASP B 209 GLY B 210 GLN B 211
SITE 5 AC2 25 HOH B3079 HOH B3114 HOH B3134 ALA C 125
SITE 6 AC2 25 MET C 127 ARG C 143 ASP C 145 ALA C 180
SITE 7 AC2 25 PHE C 182
SITE 1 AC3 23 ALA B 125 LYS B 126 MET B 127 ARG B 143
SITE 2 AC3 23 ASP B 145 ALA B 180 PHE B 182 GLY C 48
SITE 3 AC3 23 ASP C 49 GLY C 50 ARG C 54 VAL C 73
SITE 4 AC3 23 LEU C 75 ASN C 115 GLU C 116 ILE C 153
SITE 5 AC3 23 THR C 156 GLY C 157 TYR C 158 SER C 161
SITE 6 AC3 23 ASP C 209 GLY C 210 GLN C 211
SITE 1 AC4 24 ALA A 125 MET A 127 ARG A 143 ASP A 145
SITE 2 AC4 24 ALA A 180 PHE A 182 GLY D 48 ASP D 49
SITE 3 AC4 24 GLY D 50 ARG D 54 VAL D 73 ASN D 115
SITE 4 AC4 24 GLU D 116 ILE D 153 THR D 156 GLY D 157
SITE 5 AC4 24 TYR D 158 SER D 161 ASP D 209 GLY D 210
SITE 6 AC4 24 GLN D 211 HOH D3087 HOH D3099 HOH D3103
CRYST1 122.141 122.141 198.595 90.00 90.00 90.00 P 41 21 2 32
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 0.008187 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008187 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005035 0.00000
(ATOM LINES ARE NOT SHOWN.)
END