HEADER OXIDOREDUCTASE 15-AUG-05 2D1C
TITLE CRYSTAL STRUCTURE OF TT0538 PROTEIN FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: OXALOSUCCINATE DECARBOXYLASE, IDH, NADP+, -SPECIFIC ICDH,
COMPND 5 IDP;
COMPND 6 EC: 1.1.1.42;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
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: PET11A
KEYWDS DEHYDROGENASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.K.LOKANATH,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 13-JUL-11 2D1C 1 VERSN
REVDAT 2 24-FEB-09 2D1C 1 VERSN
REVDAT 1 10-OCT-06 2D1C 0
JRNL AUTH N.K.LOKANATH,N.KUNISHIMA
JRNL TITL CRYSTAL STRUCTURE OF TT0538 PROTEIN FROM THERMUS
JRNL TITL 2 THERMOPHILUS HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1792149.520
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 92029
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) : 0.207
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4617
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 14562
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 753
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7652
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 122
REMARK 3 SOLVENT ATOMS : 870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.84000
REMARK 3 B22 (A**2) : -1.70000
REMARK 3 B33 (A**2) : -0.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.21
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) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.86
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) : 1.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.730 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.780 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.550 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 45.33
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 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : LIG.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : LIG.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D1C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-05.
REMARK 100 THE RCSB ID CODE IS RCSB024865.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-05; 10-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0; NULL
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SPRING-8; SPRING-8
REMARK 200 BEAMLINE : BL26B1; BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0; 0.978954, 0.979321, 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE; GRAPHITE
REMARK 200 OPTICS : GRAPHITE; GRAPHITE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V; RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92029
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
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) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.26000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NH2SO4, PEG 4000, PH 5.6, MICROBATCH,
REMARK 280 TEMPERATURE 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 47.59200
REMARK 290 SMTRY3 2 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 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: 14880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 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 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 MET B 1
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 GLN B 363 CB CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP B 474 NE1 TRP B 474 CE2 0.111
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 132 88.01 -152.93
REMARK 500 GLU A 141 -148.59 -135.29
REMARK 500 ASP A 142 -155.75 73.07
REMARK 500 TYR A 144 0.57 -59.35
REMARK 500 MET A 195 75.74 -106.26
REMARK 500 GLU A 238 -66.08 -122.63
REMARK 500 GLU A 310 58.05 -100.83
REMARK 500 LYS A 361 -93.40 -95.91
REMARK 500 ARG A 365 57.09 -109.66
REMARK 500 PRO A 417 33.60 -82.35
REMARK 500 ASP A 442 33.49 -83.33
REMARK 500 ARG A 471 -30.92 -132.63
REMARK 500 MET A 475 -10.17 -142.37
REMARK 500 ASN B 121 19.39 57.79
REMARK 500 VAL B 122 79.78 -112.14
REMARK 500 ASP B 132 86.95 -151.67
REMARK 500 GLU B 141 -149.56 -133.63
REMARK 500 ASP B 142 -154.20 73.06
REMARK 500 TYR B 144 0.03 -60.29
REMARK 500 MET B 195 76.48 -105.52
REMARK 500 GLU B 238 -67.06 -124.24
REMARK 500 ALA B 283 73.46 38.78
REMARK 500 GLU B 310 61.03 -101.22
REMARK 500 THR B 362 73.79 -61.42
REMARK 500 GLN B 363 43.94 -93.76
REMARK 500 PRO B 417 34.33 -84.54
REMARK 500 ASP B 442 33.34 -84.96
REMARK 500 ARG B 471 -31.51 -131.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1904 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH A1981 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH B2011 DISTANCE = 5.04 ANGSTROMS
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 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 1585
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 1586
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003000538.1 RELATED DB: TARGETDB
DBREF 2D1C A 1 496 UNP P33197 IDH_THET8 1 496
DBREF 2D1C B 1 496 UNP P33197 IDH_THET8 1 496
SEQRES 1 A 496 MET PRO LEU ILE THR THR GLU THR GLY LYS LYS MET HIS
SEQRES 2 A 496 VAL LEU GLU ASP GLY ARG LYS LEU ILE THR VAL ILE PRO
SEQRES 3 A 496 GLY ASP GLY ILE GLY PRO GLU CYS VAL GLU ALA THR LEU
SEQRES 4 A 496 LYS VAL LEU GLU ALA ALA LYS ALA PRO LEU ALA TYR GLU
SEQRES 5 A 496 VAL ARG GLU ALA GLY ALA SER VAL PHE ARG ARG GLY ILE
SEQRES 6 A 496 ALA SER GLY VAL PRO GLN GLU THR ILE GLU SER ILE ARG
SEQRES 7 A 496 LYS THR ARG VAL VAL LEU LYS GLY PRO LEU GLU THR PRO
SEQRES 8 A 496 VAL GLY TYR GLY GLU LYS SER ALA ASN VAL THR LEU ARG
SEQRES 9 A 496 LYS LEU PHE GLU THR TYR ALA ASN VAL ARG PRO VAL ARG
SEQRES 10 A 496 GLU PHE PRO ASN VAL PRO THR PRO TYR ALA GLY ARG GLY
SEQRES 11 A 496 ILE ASP LEU VAL VAL VAL ARG GLU ASN VAL GLU ASP LEU
SEQRES 12 A 496 TYR ALA GLY ILE GLU HIS MET GLN THR PRO SER VAL ALA
SEQRES 13 A 496 GLN THR LEU LYS LEU ILE SER TRP LYS GLY SER GLU LYS
SEQRES 14 A 496 ILE VAL ARG PHE ALA PHE GLU LEU ALA ARG ALA GLU GLY
SEQRES 15 A 496 ARG LYS LYS VAL HIS CYS ALA THR LYS SER ASN ILE MET
SEQRES 16 A 496 LYS LEU ALA GLU GLY THR LEU LYS ARG ALA PHE GLU GLN
SEQRES 17 A 496 VAL ALA GLN GLU TYR PRO ASP ILE GLU ALA VAL HIS ILE
SEQRES 18 A 496 ILE VAL ASP ASN ALA ALA HIS GLN LEU VAL LYS ARG PRO
SEQRES 19 A 496 GLU GLN PHE GLU VAL ILE VAL THR THR ASN MET ASN GLY
SEQRES 20 A 496 ASP ILE LEU SER ASP LEU THR SER GLY LEU ILE GLY GLY
SEQRES 21 A 496 LEU GLY PHE ALA PRO SER ALA ASN ILE GLY ASN GLU VAL
SEQRES 22 A 496 ALA ILE PHE GLU ALA VAL HIS GLY SER ALA PRO LYS TYR
SEQRES 23 A 496 ALA GLY LYS ASN VAL ILE ASN PRO THR ALA VAL LEU LEU
SEQRES 24 A 496 SER ALA VAL MET MET LEU ARG TYR LEU GLU GLU PHE ALA
SEQRES 25 A 496 THR ALA ASP LEU ILE GLU ASN ALA LEU LEU TYR THR LEU
SEQRES 26 A 496 GLU GLU GLY ARG VAL LEU THR GLY ASP VAL VAL GLY TYR
SEQRES 27 A 496 ASP ARG GLY ALA LYS THR THR GLU TYR THR GLU ALA ILE
SEQRES 28 A 496 ILE GLN ASN LEU GLY LYS THR PRO ARG LYS THR GLN VAL
SEQRES 29 A 496 ARG GLY TYR LYS PRO PHE ARG LEU PRO GLN VAL ASP GLY
SEQRES 30 A 496 ALA ILE ALA PRO ILE VAL PRO ARG SER ARG ARG VAL VAL
SEQRES 31 A 496 GLY VAL ASP VAL PHE VAL GLU THR ASN LEU LEU PRO GLU
SEQRES 32 A 496 ALA LEU GLY LYS ALA LEU GLU ASP LEU ALA ALA GLY THR
SEQRES 33 A 496 PRO PHE ARG LEU LYS MET ILE SER ASN ARG GLY THR GLN
SEQRES 34 A 496 VAL TYR PRO PRO THR GLY GLY LEU THR ASP LEU VAL ASP
SEQRES 35 A 496 HIS TYR ARG CYS ARG PHE LEU TYR THR GLY GLU GLY GLU
SEQRES 36 A 496 ALA LYS ASP PRO GLU ILE LEU ASP LEU VAL SER ARG VAL
SEQRES 37 A 496 ALA SER ARG PHE ARG TRP MET HIS LEU GLU LYS LEU GLN
SEQRES 38 A 496 GLU PHE ASP GLY GLU PRO GLY PHE THR LYS ALA GLN GLY
SEQRES 39 A 496 GLU ASP
SEQRES 1 B 496 MET PRO LEU ILE THR THR GLU THR GLY LYS LYS MET HIS
SEQRES 2 B 496 VAL LEU GLU ASP GLY ARG LYS LEU ILE THR VAL ILE PRO
SEQRES 3 B 496 GLY ASP GLY ILE GLY PRO GLU CYS VAL GLU ALA THR LEU
SEQRES 4 B 496 LYS VAL LEU GLU ALA ALA LYS ALA PRO LEU ALA TYR GLU
SEQRES 5 B 496 VAL ARG GLU ALA GLY ALA SER VAL PHE ARG ARG GLY ILE
SEQRES 6 B 496 ALA SER GLY VAL PRO GLN GLU THR ILE GLU SER ILE ARG
SEQRES 7 B 496 LYS THR ARG VAL VAL LEU LYS GLY PRO LEU GLU THR PRO
SEQRES 8 B 496 VAL GLY TYR GLY GLU LYS SER ALA ASN VAL THR LEU ARG
SEQRES 9 B 496 LYS LEU PHE GLU THR TYR ALA ASN VAL ARG PRO VAL ARG
SEQRES 10 B 496 GLU PHE PRO ASN VAL PRO THR PRO TYR ALA GLY ARG GLY
SEQRES 11 B 496 ILE ASP LEU VAL VAL VAL ARG GLU ASN VAL GLU ASP LEU
SEQRES 12 B 496 TYR ALA GLY ILE GLU HIS MET GLN THR PRO SER VAL ALA
SEQRES 13 B 496 GLN THR LEU LYS LEU ILE SER TRP LYS GLY SER GLU LYS
SEQRES 14 B 496 ILE VAL ARG PHE ALA PHE GLU LEU ALA ARG ALA GLU GLY
SEQRES 15 B 496 ARG LYS LYS VAL HIS CYS ALA THR LYS SER ASN ILE MET
SEQRES 16 B 496 LYS LEU ALA GLU GLY THR LEU LYS ARG ALA PHE GLU GLN
SEQRES 17 B 496 VAL ALA GLN GLU TYR PRO ASP ILE GLU ALA VAL HIS ILE
SEQRES 18 B 496 ILE VAL ASP ASN ALA ALA HIS GLN LEU VAL LYS ARG PRO
SEQRES 19 B 496 GLU GLN PHE GLU VAL ILE VAL THR THR ASN MET ASN GLY
SEQRES 20 B 496 ASP ILE LEU SER ASP LEU THR SER GLY LEU ILE GLY GLY
SEQRES 21 B 496 LEU GLY PHE ALA PRO SER ALA ASN ILE GLY ASN GLU VAL
SEQRES 22 B 496 ALA ILE PHE GLU ALA VAL HIS GLY SER ALA PRO LYS TYR
SEQRES 23 B 496 ALA GLY LYS ASN VAL ILE ASN PRO THR ALA VAL LEU LEU
SEQRES 24 B 496 SER ALA VAL MET MET LEU ARG TYR LEU GLU GLU PHE ALA
SEQRES 25 B 496 THR ALA ASP LEU ILE GLU ASN ALA LEU LEU TYR THR LEU
SEQRES 26 B 496 GLU GLU GLY ARG VAL LEU THR GLY ASP VAL VAL GLY TYR
SEQRES 27 B 496 ASP ARG GLY ALA LYS THR THR GLU TYR THR GLU ALA ILE
SEQRES 28 B 496 ILE GLN ASN LEU GLY LYS THR PRO ARG LYS THR GLN VAL
SEQRES 29 B 496 ARG GLY TYR LYS PRO PHE ARG LEU PRO GLN VAL ASP GLY
SEQRES 30 B 496 ALA ILE ALA PRO ILE VAL PRO ARG SER ARG ARG VAL VAL
SEQRES 31 B 496 GLY VAL ASP VAL PHE VAL GLU THR ASN LEU LEU PRO GLU
SEQRES 32 B 496 ALA LEU GLY LYS ALA LEU GLU ASP LEU ALA ALA GLY THR
SEQRES 33 B 496 PRO PHE ARG LEU LYS MET ILE SER ASN ARG GLY THR GLN
SEQRES 34 B 496 VAL TYR PRO PRO THR GLY GLY LEU THR ASP LEU VAL ASP
SEQRES 35 B 496 HIS TYR ARG CYS ARG PHE LEU TYR THR GLY GLU GLY GLU
SEQRES 36 B 496 ALA LYS ASP PRO GLU ILE LEU ASP LEU VAL SER ARG VAL
SEQRES 37 B 496 ALA SER ARG PHE ARG TRP MET HIS LEU GLU LYS LEU GLN
SEQRES 38 B 496 GLU PHE ASP GLY GLU PRO GLY PHE THR LYS ALA GLN GLY
SEQRES 39 B 496 GLU ASP
HET NAP A1002 48
HET NAP B1003 48
HET CIT A1585 13
HET CIT B1586 13
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM CIT CITRIC ACID
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 5 CIT 2(C6 H8 O7)
FORMUL 7 HOH *870(H2 O)
HELIX 1 1 ILE A 30 ALA A 45 1 16
HELIX 2 2 GLY A 57 ARG A 62 1 6
HELIX 3 3 PRO A 70 ARG A 81 1 12
HELIX 4 4 SER A 98 PHE A 107 1 10
HELIX 5 5 ASP A 142 GLY A 146 5 5
HELIX 6 6 TRP A 164 GLU A 181 1 18
HELIX 7 7 LEU A 197 GLN A 211 1 15
HELIX 8 8 VAL A 223 ARG A 233 1 11
HELIX 9 9 PRO A 234 PHE A 237 5 4
HELIX 10 10 THR A 243 GLY A 256 1 14
HELIX 11 11 GLY A 260 PHE A 263 5 4
HELIX 12 12 PRO A 294 LEU A 308 1 15
HELIX 13 13 GLU A 310 GLY A 328 1 19
HELIX 14 14 THR A 332 GLY A 337 1 6
HELIX 15 15 LYS A 343 ASN A 354 1 12
HELIX 16 16 GLN A 374 ALA A 378 5 5
HELIX 17 17 LEU A 401 ALA A 414 1 14
HELIX 18 18 LYS A 457 SER A 470 1 14
HELIX 19 19 ILE B 30 ALA B 45 1 16
HELIX 20 20 GLY B 57 ARG B 62 1 6
HELIX 21 21 PRO B 70 ARG B 81 1 12
HELIX 22 22 SER B 98 PHE B 107 1 10
HELIX 23 23 ASP B 142 GLY B 146 5 5
HELIX 24 24 TRP B 164 GLU B 181 1 18
HELIX 25 25 LEU B 197 GLN B 211 1 15
HELIX 26 26 VAL B 223 ARG B 233 1 11
HELIX 27 27 PRO B 234 PHE B 237 5 4
HELIX 28 28 THR B 243 GLY B 256 1 14
HELIX 29 29 GLY B 260 PHE B 263 5 4
HELIX 30 30 ALA B 283 ALA B 287 5 5
HELIX 31 31 PRO B 294 LEU B 308 1 15
HELIX 32 32 GLU B 310 GLY B 328 1 19
HELIX 33 33 THR B 332 GLY B 337 1 6
HELIX 34 34 LYS B 343 ASN B 354 1 12
HELIX 35 35 GLN B 374 ALA B 378 5 5
HELIX 36 36 LEU B 401 ALA B 414 1 14
HELIX 37 37 LYS B 457 SER B 470 1 14
SHEET 1 A 4 LEU A 3 THR A 5 0
SHEET 2 A 4 LYS A 11 VAL A 14 -1 O MET A 12 N ILE A 4
SHEET 3 A 4 LYS A 20 ILE A 25 -1 O LEU A 21 N HIS A 13
SHEET 4 A 4 LEU A 49 VAL A 53 1 O GLU A 52 N VAL A 24
SHEET 1 B11 LEU A 3 THR A 5 0
SHEET 2 B11 LYS A 11 VAL A 14 -1 O MET A 12 N ILE A 4
SHEET 3 B11 LYS A 20 ILE A 25 -1 O LEU A 21 N HIS A 13
SHEET 4 B11 VAL A 82 LYS A 85 1 O VAL A 82 N THR A 23
SHEET 5 B11 ALA A 274 ALA A 278 1 O PHE A 276 N VAL A 83
SHEET 6 B11 PRO A 265 ILE A 269 -1 N ASN A 268 O ILE A 275
SHEET 7 B11 ALA A 111 ARG A 117 -1 N ALA A 111 O ILE A 269
SHEET 8 B11 ASP A 132 GLU A 138 -1 O ARG A 137 N ASN A 112
SHEET 9 B11 VAL A 239 THR A 242 1 O ILE A 240 N VAL A 136
SHEET 10 B11 LYS A 185 THR A 190 1 N HIS A 187 O VAL A 239
SHEET 11 B11 GLU A 217 ILE A 222 1 O ILE A 221 N CYS A 188
SHEET 1 C 4 GLU A 148 THR A 152 0
SHEET 2 C 4 VAL A 155 SER A 163 -1 O GLN A 157 N HIS A 149
SHEET 3 C 4 VAL B 155 SER B 163 -1 O ALA B 156 N ILE A 162
SHEET 4 C 4 GLU B 148 THR B 152 -1 N HIS B 149 O GLN B 157
SHEET 1 D10 THR A 428 TYR A 431 0
SHEET 2 D10 PHE A 418 ASN A 425 -1 N ILE A 423 O VAL A 430
SHEET 3 D10 HIS A 443 TYR A 450 -1 O ARG A 447 N LYS A 421
SHEET 4 D10 ARG A 387 GLU A 397 -1 N VAL A 390 O TYR A 450
SHEET 5 D10 ARG A 473 PHE A 483 -1 O GLU A 478 N ASP A 393
SHEET 6 D10 ARG B 473 PHE B 483 -1 O MET B 475 N LYS A 479
SHEET 7 D10 ARG B 387 GLU B 397 -1 N ASP B 393 O GLU B 478
SHEET 8 D10 HIS B 443 TYR B 450 -1 O TYR B 450 N VAL B 390
SHEET 9 D10 PHE B 418 ASN B 425 -1 N LYS B 421 O ARG B 447
SHEET 10 D10 THR B 428 TYR B 431 -1 O VAL B 430 N ILE B 423
SHEET 1 E 4 GLU A 486 PRO A 487 0
SHEET 2 E 4 ARG A 473 PHE A 483 -1 N PHE A 483 O GLU A 486
SHEET 3 E 4 ARG B 473 PHE B 483 -1 O MET B 475 N LYS A 479
SHEET 4 E 4 GLU B 486 PRO B 487 -1 O GLU B 486 N PHE B 483
SHEET 1 F 4 LEU B 3 THR B 5 0
SHEET 2 F 4 LYS B 11 VAL B 14 -1 O MET B 12 N ILE B 4
SHEET 3 F 4 LYS B 20 ILE B 25 -1 O LEU B 21 N HIS B 13
SHEET 4 F 4 LEU B 49 VAL B 53 1 O ALA B 50 N ILE B 22
SHEET 1 G11 LEU B 3 THR B 5 0
SHEET 2 G11 LYS B 11 VAL B 14 -1 O MET B 12 N ILE B 4
SHEET 3 G11 LYS B 20 ILE B 25 -1 O LEU B 21 N HIS B 13
SHEET 4 G11 VAL B 82 LYS B 85 1 O VAL B 82 N THR B 23
SHEET 5 G11 ALA B 274 ALA B 278 1 O PHE B 276 N VAL B 83
SHEET 6 G11 PRO B 265 ILE B 269 -1 N ASN B 268 O ILE B 275
SHEET 7 G11 ALA B 111 ARG B 117 -1 N ALA B 111 O ILE B 269
SHEET 8 G11 ASP B 132 GLU B 138 -1 O LEU B 133 N VAL B 116
SHEET 9 G11 VAL B 239 THR B 242 1 O ILE B 240 N VAL B 136
SHEET 10 G11 LYS B 185 THR B 190 1 N HIS B 187 O VAL B 239
SHEET 11 G11 GLU B 217 ILE B 222 1 O VAL B 219 N CYS B 188
CISPEP 1 TYR A 431 PRO A 432 0 -0.14
CISPEP 2 TYR B 431 PRO B 432 0 -0.28
SITE 1 AC1 33 LYS A 85 PRO A 87 LEU A 88 GLU A 89
SITE 2 AC1 33 THR A 90 ASN A 100 LEU A 261 GLU A 277
SITE 3 AC1 33 VAL A 279 HIS A 280 GLY A 281 SER A 282
SITE 4 AC1 33 ALA A 283 LYS A 285 TYR A 286 ILE A 292
SITE 5 AC1 33 ASN A 293 ASP A 334 CIT A1585 HOH A1618
SITE 6 AC1 33 HOH A1717 HOH A1800 HOH A1810 HOH A1839
SITE 7 AC1 33 HOH A1975 ASN B 193 ILE B 222 ASN B 225
SITE 8 AC1 33 HIS B 228 GLN B 229 LYS B 232 HOH B1669
SITE 9 AC1 33 HOH B1975
SITE 1 AC2 32 ASN A 193 ILE A 222 ASN A 225 GLN A 229
SITE 2 AC2 32 LYS A 232 HOH A1625 HOH A1759 LYS B 85
SITE 3 AC2 32 PRO B 87 LEU B 88 GLU B 89 THR B 90
SITE 4 AC2 32 ASN B 100 LEU B 261 GLU B 277 VAL B 279
SITE 5 AC2 32 HIS B 280 GLY B 281 SER B 282 ALA B 283
SITE 6 AC2 32 LYS B 285 TYR B 286 ILE B 292 ASN B 293
SITE 7 AC2 32 ASP B 334 CIT B1586 HOH B1612 HOH B1687
SITE 8 AC2 32 HOH B1711 HOH B1745 HOH B1816 HOH B1840
SITE 1 AC3 14 THR A 90 SER A 98 ASN A 100 ARG A 104
SITE 2 AC3 14 ARG A 114 ARG A 137 TYR A 144 ASP A 248
SITE 3 AC3 14 NAP A1002 LYS B 191 ASN B 193 ASP B 224
SITE 4 AC3 14 HOH B1693 HOH B1854
SITE 1 AC4 14 LYS A 191 ASN A 193 ASP A 224 THR B 90
SITE 2 AC4 14 SER B 98 ASN B 100 ARG B 104 ARG B 114
SITE 3 AC4 14 ARG B 137 TYR B 144 ASP B 248 NAP B1003
SITE 4 AC4 14 HOH B1688 HOH B1698
CRYST1 73.022 95.184 72.989 90.00 92.07 90.00 P 1 21 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 0.013695 0.000000 0.000495 0.00000
SCALE2 0.000000 0.010506 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013710 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
