HEADER OXIDOREDUCTASE 08-APR-04 1T09
TITLE CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC NADP(+)-DEPENDENT ISOCITRATE
TITLE 2 DEHYDROGENASE IN COMPLEX NADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP] CYTOPLASMIC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYTOSOLIC NADP(+)-DEPENDENT ISOCITRATE DEHYDROGENASE,
COMPND 5 OXALOSUCCINATE DECARBOXYLASE, IDH, NADP+-SPECIFIC ICDH, IDP;
COMPND 6 EC: 1.1.1.42;
COMPND 7 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: IDH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22B(+)
KEYWDS ROSSMANN FOLD, PROTEIN-COFACTOR COMPLEX, NADP, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.XU,J.ZHAO,B.PENG,Q.HUANG,E.ARNOLD,J.DING
REVDAT 4 25-OCT-23 1T09 1 REMARK
REVDAT 3 24-FEB-09 1T09 1 VERSN
REVDAT 2 07-SEP-04 1T09 1 JRNL
REVDAT 1 15-JUN-04 1T09 0
JRNL AUTH X.XU,J.ZHAO,Z.XU,B.PENG,Q.HUANG,E.ARNOLD,J.DING
JRNL TITL STRUCTURES OF HUMAN CYTOSOLIC NADP-DEPENDENT ISOCITRATE
JRNL TITL 2 DEHYDROGENASE REVEAL A NOVEL SELF-REGULATORY MECHANISM OF
JRNL TITL 3 ACTIVITY
JRNL REF J.BIOL.CHEM. V. 279 33946 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15173171
JRNL DOI 10.1074/JBC.M404298200
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2335794.040
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 30393
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) : 0.210
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1529
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4649
REMARK 3 BIN R VALUE (WORKING SET) : 0.2731
REMARK 3 BIN FREE R VALUE : 0.3107
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 236
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6556
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.00000
REMARK 3 B22 (A**2) : 2.62000
REMARK 3 B33 (A**2) : -5.62000
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) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.32
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) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
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 : 0.32
REMARK 3 BSOL : 20.25
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NDP.PARAM
REMARK 3 PARAMETER FILE 5 : ICT.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NDP.TOP
REMARK 3 TOPOLOGY FILE 5 : ICT.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T09 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022150.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-03
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 : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : GRAPHITE
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 : 30445
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.38600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.300
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: PDB ENTRY 1LWD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, MES, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 154.01500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.35500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.35500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 231.02250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.35500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.35500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 77.00750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.35500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.35500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 231.02250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.35500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.35500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 77.00750
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 154.01500
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 BIOLOGICAL ASSEMBLY IS AN ASYMMETRIC HOMODIMER.
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: 7890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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 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 470 MET B 1 CG SD CE
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 SER A 2 -104.40 -87.66
REMARK 500 GLU A 17 -129.30 36.40
REMARK 500 ASN A 68 -24.68 67.97
REMARK 500 GLN A 90 146.42 166.13
REMARK 500 SER A 122 -38.82 -37.22
REMARK 500 THR A 142 68.14 -118.52
REMARK 500 VAL A 146 97.69 72.14
REMARK 500 PRO A 149 159.52 -36.94
REMARK 500 GLN A 163 122.87 -39.01
REMARK 500 LEU A 168 96.82 64.72
REMARK 500 HIS A 170 141.96 -176.31
REMARK 500 TYR A 235 -62.12 72.01
REMARK 500 GLU A 247 138.03 -177.16
REMARK 500 ILE A 251 -37.18 -34.31
REMARK 500 VAL A 281 -66.18 -108.04
REMARK 500 ALA A 282 111.42 145.12
REMARK 500 GLN A 283 -70.84 -33.60
REMARK 500 SER B 2 -104.07 -105.42
REMARK 500 GLU B 17 -131.97 36.19
REMARK 500 ASN B 68 -2.21 60.64
REMARK 500 GLN B 90 146.89 -176.05
REMARK 500 ASP B 137 -141.12 45.87
REMARK 500 ARG B 140 148.97 -171.28
REMARK 500 PRO B 158 154.18 -49.93
REMARK 500 ASP B 160 37.00 -82.24
REMARK 500 HIS B 170 149.29 -178.01
REMARK 500 ASN B 213 3.87 -61.13
REMARK 500 LEU B 216 73.64 -109.04
REMARK 500 GLN B 234 -6.47 -141.65
REMARK 500 LYS B 260 42.35 -86.97
REMARK 500 ASP B 273 -160.72 55.31
REMARK 500 ASP B 275 -142.56 -166.55
REMARK 500 GLN B 277 -179.93 -173.93
REMARK 500 ASP B 279 -79.18 -83.31
REMARK 500 ASP B 299 -1.14 -56.20
REMARK 500 HIS B 309 -173.41 -69.81
REMARK 500 ASN B 349 79.80 -109.66
REMARK 500 ALA B 377 -50.04 75.36
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 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 1003
DBREF 1T09 A 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 1T09 B 1 414 UNP O75874 IDHC_HUMAN 1 414
SEQRES 1 A 414 MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET
SEQRES 2 A 414 GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE
SEQRES 3 A 414 LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU
SEQRES 4 A 414 HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR
SEQRES 5 A 414 ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS
SEQRES 6 A 414 LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO
SEQRES 7 A 414 ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET
SEQRES 8 A 414 TRP LYS SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY
SEQRES 9 A 414 GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE
SEQRES 10 A 414 PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE
SEQRES 11 A 414 GLY ARG HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP
SEQRES 12 A 414 PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR
SEQRES 13 A 414 THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL
SEQRES 14 A 414 HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET
SEQRES 15 A 414 TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER
SEQRES 16 A 414 SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR
SEQRES 17 A 414 LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY
SEQRES 18 A 414 ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN
SEQRES 19 A 414 TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU
SEQRES 20 A 414 HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS
SEQRES 21 A 414 SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP
SEQRES 22 A 414 GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY
SEQRES 23 A 414 SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP
SEQRES 24 A 414 GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL
SEQRES 25 A 414 THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR
SEQRES 26 A 414 SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG
SEQRES 27 A 414 GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU
SEQRES 28 A 414 LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE
SEQRES 29 A 414 GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA
SEQRES 30 A 414 ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP
SEQRES 31 A 414 TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU
SEQRES 32 A 414 ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU
SEQRES 1 B 414 MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET
SEQRES 2 B 414 GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE
SEQRES 3 B 414 LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU
SEQRES 4 B 414 HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR
SEQRES 5 B 414 ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS
SEQRES 6 B 414 LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO
SEQRES 7 B 414 ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET
SEQRES 8 B 414 TRP LYS SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY
SEQRES 9 B 414 GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE
SEQRES 10 B 414 PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE
SEQRES 11 B 414 GLY ARG HIS ALA TYR GLY ASP GLN TYR ARG ALA THR ASP
SEQRES 12 B 414 PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR
SEQRES 13 B 414 THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL
SEQRES 14 B 414 HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET
SEQRES 15 B 414 TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER
SEQRES 16 B 414 SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR
SEQRES 17 B 414 LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY
SEQRES 18 B 414 ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN
SEQRES 19 B 414 TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU
SEQRES 20 B 414 HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS
SEQRES 21 B 414 SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP
SEQRES 22 B 414 GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY
SEQRES 23 B 414 SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP
SEQRES 24 B 414 GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL
SEQRES 25 B 414 THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR
SEQRES 26 B 414 SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG
SEQRES 27 B 414 GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU
SEQRES 28 B 414 LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE
SEQRES 29 B 414 GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA
SEQRES 30 B 414 ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP
SEQRES 31 B 414 TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU
SEQRES 32 B 414 ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU
HET NAP A 415 48
HET NAP B1003 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 *155(H2 O)
HELIX 1 1 ASP A 16 LEU A 30 1 15
HELIX 2 2 GLY A 45 THR A 52 1 8
HELIX 3 3 ASP A 54 ASN A 68 1 15
HELIX 4 4 ASP A 79 PHE A 86 1 8
HELIX 5 5 SER A 94 GLY A 104 1 11
HELIX 6 6 ASP A 186 GLY A 204 1 19
HELIX 7 7 LYS A 218 GLN A 234 1 17
HELIX 8 8 TYR A 235 GLN A 242 1 8
HELIX 9 9 ILE A 251 LYS A 260 1 10
HELIX 10 10 SER A 287 GLY A 289 5 3
HELIX 11 11 VAL A 312 LYS A 321 1 10
HELIX 12 12 PRO A 329 ASN A 348 1 20
HELIX 13 13 ASN A 349 ALA A 369 1 21
HELIX 14 14 THR A 373 GLY A 382 1 10
HELIX 15 15 LEU A 383 VAL A 386 5 4
HELIX 16 16 GLN A 387 TYR A 391 5 5
HELIX 17 17 ASN A 393 LYS A 413 1 21
HELIX 18 18 ASP B 16 ILE B 31 1 16
HELIX 19 19 GLY B 45 THR B 52 1 8
HELIX 20 20 ASP B 54 ASN B 68 1 15
HELIX 21 21 ASP B 79 PHE B 86 1 8
HELIX 22 22 SER B 94 GLY B 104 1 11
HELIX 23 23 ASP B 186 LYS B 203 1 18
HELIX 24 24 LYS B 218 TYR B 235 1 18
HELIX 25 25 TYR B 235 GLN B 242 1 8
HELIX 26 26 LEU B 250 LYS B 260 1 11
HELIX 27 27 ASP B 279 GLY B 284 1 6
HELIX 28 28 SER B 287 GLY B 289 5 3
HELIX 29 29 VAL B 312 LYS B 321 1 10
HELIX 30 30 PRO B 329 ASN B 348 1 20
HELIX 31 31 ASN B 349 ALA B 369 1 21
HELIX 32 32 LYS B 374 GLY B 382 1 9
HELIX 33 33 LEU B 383 VAL B 386 5 4
HELIX 34 34 GLN B 387 TYR B 391 5 5
HELIX 35 35 ASN B 393 LEU B 414 1 22
SHEET 1 A10 VAL A 35 ASP A 43 0
SHEET 2 A10 ILE A 5 GLN A 14 1 N GLY A 8 O ASP A 38
SHEET 3 A10 VAL A 69 LYS A 72 1 O VAL A 71 N VAL A 11
SHEET 4 A10 VAL A 303 ALA A 307 1 O ALA A 305 N LYS A 72
SHEET 5 A10 MET A 291 VAL A 296 -1 N LEU A 295 O GLU A 304
SHEET 6 A10 THR A 106 ALA A 111 -1 N GLU A 110 O THR A 292
SHEET 7 A10 LYS A 126 ARG A 132 -1 O ILE A 130 N ARG A 109
SHEET 8 A10 GLY A 263 CYS A 269 1 O TRP A 267 N ILE A 129
SHEET 9 A10 LEU A 207 THR A 211 1 N TYR A 208 O ALA A 268
SHEET 10 A10 HIS A 248 LEU A 250 1 O ARG A 249 N LEU A 209
SHEET 1 B 2 ALA A 134 TYR A 135 0
SHEET 2 B 2 ASP A 275 VAL A 276 1 O ASP A 275 N TYR A 135
SHEET 1 C 4 THR A 142 PHE A 144 0
SHEET 2 C 4 GLY A 177 GLN A 185 -1 O ALA A 179 N PHE A 144
SHEET 3 C 4 GLY B 177 GLN B 185 -1 O VAL B 178 N ASN A 184
SHEET 4 C 4 THR B 142 VAL B 146 -1 N THR B 142 O GLY B 181
SHEET 1 D 3 VAL A 165 THR A 166 0
SHEET 2 D 3 GLY A 150 PRO A 158 -1 N TYR A 156 O VAL A 165
SHEET 3 D 3 HIS A 170 PHE A 172 -1 O HIS A 170 N VAL A 152
SHEET 1 E 4 VAL A 165 THR A 166 0
SHEET 2 E 4 GLY A 150 PRO A 158 -1 N TYR A 156 O VAL A 165
SHEET 3 E 4 GLY B 150 PRO B 158 -1 O THR B 157 N LYS A 151
SHEET 4 E 4 VAL B 165 PHE B 172 -1 O VAL B 165 N TYR B 156
SHEET 1 F10 VAL B 35 ASP B 43 0
SHEET 2 F10 ILE B 5 GLN B 14 1 N GLY B 8 O ASP B 38
SHEET 3 F10 VAL B 69 LYS B 72 1 O VAL B 71 N VAL B 11
SHEET 4 F10 VAL B 303 ALA B 307 1 O ALA B 305 N GLY B 70
SHEET 5 F10 MET B 291 VAL B 296 -1 N LEU B 295 O GLU B 304
SHEET 6 F10 THR B 106 ALA B 111 -1 N GLU B 110 O THR B 292
SHEET 7 F10 LYS B 126 ARG B 132 -1 O ILE B 130 N ARG B 109
SHEET 8 F10 GLY B 263 CYS B 269 1 O CYS B 269 N GLY B 131
SHEET 9 F10 LEU B 207 SER B 210 1 N TYR B 208 O ILE B 266
SHEET 10 F10 TYR B 246 HIS B 248 1 O GLU B 247 N LEU B 207
SITE 1 AC1 19 LYS A 72 ALA A 74 THR A 75 ILE A 76
SITE 2 AC1 19 THR A 77 ARG A 82 ASN A 96 ASP A 279
SITE 3 AC1 19 SER A 280 LEU A 288 HIS A 309 GLY A 310
SITE 4 AC1 19 THR A 311 VAL A 312 ARG A 314 HIS A 315
SITE 5 AC1 19 THR A 327 ASN A 328 HOH A 501
SITE 1 AC2 17 LYS B 72 ALA B 74 THR B 75 ILE B 76
SITE 2 AC2 17 THR B 77 ARG B 82 ASN B 96 LEU B 288
SITE 3 AC2 17 HIS B 309 GLY B 310 THR B 311 VAL B 312
SITE 4 AC2 17 ARG B 314 HIS B 315 ASN B 328 HOH B1024
SITE 5 AC2 17 HOH B1025
CRYST1 82.710 82.710 308.030 90.00 90.00 90.00 P 43 21 2 16
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 0.012090 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012090 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003246 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
