HEADER OXIDOREDUCTASE,HYDROLASE 29-NOV-99 1DIA
TITLE HUMAN METHYLENETETRAHYDROFOLATE DEHYDROGENASE / CYCLOHYDROLASE
TITLE 2 COMPLEXED WITH NADP AND INHIBITOR LY249543
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLENETETRAHYDROFOLATE DEHYDROGENASE/CYCLOHYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DC301;
COMPND 5 EC: 1.5.1.5, 3.5.4.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TETRAHYDROFOLATE, DEHYDROGENASE, CYCLOHYDROLASE, NADP, INHIBITOR,
KEYWDS 2 ROSSMANN FOLD, OXIDOREDUCTASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHMIDT,H.WU,R.E.MACKENZIE,V.J.CHEN,J.R.BEWLY,J.E.RAY,J.E.TOTH,
AUTHOR 2 M.CYGLER
REVDAT 5 07-FEB-24 1DIA 1 REMARK
REVDAT 4 31-JAN-18 1DIA 1 REMARK
REVDAT 3 24-FEB-09 1DIA 1 VERSN
REVDAT 2 09-OCT-02 1DIA 1 REMARK HETATM MASTER
REVDAT 1 05-JUL-00 1DIA 0
JRNL AUTH A.SCHMIDT,H.WU,R.E.MACKENZIE,V.J.CHEN,J.R.BEWLY,J.E.RAY,
JRNL AUTH 2 J.E.TOTH,M.CYGLER
JRNL TITL STRUCTURES OF THREE INHIBITOR COMPLEXES PROVIDE INSIGHT INTO
JRNL TITL 2 THE REACTION MECHANISM OF THE HUMAN
JRNL TITL 3 METHYLENETETRAHYDROFOLATE DEHYDROGENASE/CYCLOHYDROLASE.
JRNL REF BIOCHEMISTRY V. 39 6325 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10828945
JRNL DOI 10.1021/BI992734Y
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.ALLAIRE,Y.LI,R.E.MACKENZIE,M.CYGLER
REMARK 1 TITL THE 3-D STRUCTURE OF A FOLATE-DEPENDENT
REMARK 1 TITL 2 DEHYDROGENASE/CYCLOHYDROLASE BIFUNCTIONAL ENZYME AT 1.5 A
REMARK 1 TITL 3 RESOLUTION
REMARK 1 REF STRUCTURE V. 6 173 1998
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(98)00019-7
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
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) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 29674
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2884
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 : 4396
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 128
REMARK 3 SOLVENT ATOMS : 195
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT CORRECTION APPLIED
REMARK 4
REMARK 4 1DIA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000010110.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAR-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 29674
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.14600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 42.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, GLYCEROL, SODIUM CITRATE,
REMARK 280 AMMONIUM ACETATE, PH 5.2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 20K, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 33.93550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.82450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 68.19800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.82450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.93550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 68.19800
REMARK 290 SMTRY3 4 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 300 REMARK: DC301 FORMS DIMERS, THE TWO MONOMERS (CHAINS A AND B) BEING
REMARK 300 RELATED BY A NONCRYSTALLOGRAPHIC TWOFOLD AXIS IN THE CRYSTAL
REMARK 300 STRUCTURE.
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: 4920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 VAL A 241
REMARK 465 PRO A 242
REMARK 465 ASP A 243
REMARK 465 ASP A 244
REMARK 465 LYS A 245
REMARK 465 LYS A 246
REMARK 465 PRO A 247
REMARK 465 ASN A 248
REMARK 465 GLY A 249
REMARK 465 ARG A 250
REMARK 465 LYS A 297
REMARK 465 PHE A 298
REMARK 465 LYS A 299
REMARK 465 PRO A 300
REMARK 465 GLY A 301
REMARK 465 LYS A 302
REMARK 465 TRP A 303
REMARK 465 MET A 304
REMARK 465 ILE A 305
REMARK 465 GLN A 306
REMARK 465 MET B 1001
REMARK 465 LYS B 1297
REMARK 465 PHE B 1298
REMARK 465 LYS B 1299
REMARK 465 PRO B 1300
REMARK 465 GLY B 1301
REMARK 465 LYS B 1302
REMARK 465 TRP B 1303
REMARK 465 MET B 1304
REMARK 465 ILE B 1305
REMARK 465 GLN B 1306
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 LYS A 83 CG CD CE NZ
REMARK 480 LYS A 251 CG CD CE NZ
REMARK 480 GLU A 296 CG CD OE1 OE2
REMARK 480 GLU B 1296 CG CD OE1 OE2
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 ASN A 45 44.02 -153.72
REMARK 500 VAL A 177 -70.62 -129.43
REMARK 500 ASN B1045 40.17 -146.20
REMARK 500 ARG B1173 38.80 -140.11
REMARK 500 VAL B1177 -73.52 -126.25
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 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE L24 A 3001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A4I RELATED DB: PDB
REMARK 900 STRUCTURE OF THE NATIVE HUMAN METHYLENETETRAHYDROFOLATE
REMARK 900 DEHYDROGENASE/ CYCLOHYDROLASE (DC301) COMPLEXED WITH THE COFACTOR
REMARK 900 NADP
REMARK 900 RELATED ID: 1DIB RELATED DB: PDB
REMARK 900 RELATED ID: 1DIG RELATED DB: PDB
DBREF 1DIA A 1 306 UNP P11586 C1TC_HUMAN 1 306
DBREF 1DIA B 1001 1306 UNP P11586 C1TC_HUMAN 1 306
SEQRES 1 A 306 MET ALA PRO ALA GLU ILE LEU ASN GLY LYS GLU ILE SER
SEQRES 2 A 306 ALA GLN ILE ARG ALA ARG LEU LYS ASN GLN VAL THR GLN
SEQRES 3 A 306 LEU LYS GLU GLN VAL PRO GLY PHE THR PRO ARG LEU ALA
SEQRES 4 A 306 ILE LEU GLN VAL GLY ASN ARG ASP ASP SER ASN LEU TYR
SEQRES 5 A 306 ILE ASN VAL LYS LEU LYS ALA ALA GLU GLU ILE GLY ILE
SEQRES 6 A 306 LYS ALA THR HIS ILE LYS LEU PRO ARG THR THR THR GLU
SEQRES 7 A 306 SER GLU VAL MET LYS TYR ILE THR SER LEU ASN GLU ASP
SEQRES 8 A 306 SER THR VAL HIS GLY PHE LEU VAL GLN LEU PRO LEU ASP
SEQRES 9 A 306 SER GLU ASN SER ILE ASN THR GLU GLU VAL ILE ASN ALA
SEQRES 10 A 306 ILE ALA PRO GLU LYS ASP VAL ASP GLY LEU THR SER ILE
SEQRES 11 A 306 ASN ALA GLY ARG LEU ALA ARG GLY ASP LEU ASN ASP CYS
SEQRES 12 A 306 PHE ILE PRO CYS THR PRO LYS GLY CYS LEU GLU LEU ILE
SEQRES 13 A 306 LYS GLU THR GLY VAL PRO ILE ALA GLY ARG HIS ALA VAL
SEQRES 14 A 306 VAL VAL GLY ARG SER LYS ILE VAL GLY ALA PRO MET HIS
SEQRES 15 A 306 ASP LEU LEU LEU TRP ASN ASN ALA THR VAL THR THR CYS
SEQRES 16 A 306 HIS SER LYS THR ALA HIS LEU ASP GLU GLU VAL ASN LYS
SEQRES 17 A 306 GLY ASP ILE LEU VAL VAL ALA THR GLY GLN PRO GLU MET
SEQRES 18 A 306 VAL LYS GLY GLU TRP ILE LYS PRO GLY ALA ILE VAL ILE
SEQRES 19 A 306 ASP CYS GLY ILE ASN TYR VAL PRO ASP ASP LYS LYS PRO
SEQRES 20 A 306 ASN GLY ARG LYS VAL VAL GLY ASP VAL ALA TYR ASP GLU
SEQRES 21 A 306 ALA LYS GLU ARG ALA SER PHE ILE THR PRO VAL PRO GLY
SEQRES 22 A 306 GLY VAL GLY PRO MET THR VAL ALA MET LEU MET GLN SER
SEQRES 23 A 306 THR VAL GLU SER ALA LYS ARG PHE LEU GLU LYS PHE LYS
SEQRES 24 A 306 PRO GLY LYS TRP MET ILE GLN
SEQRES 1 B 306 MET ALA PRO ALA GLU ILE LEU ASN GLY LYS GLU ILE SER
SEQRES 2 B 306 ALA GLN ILE ARG ALA ARG LEU LYS ASN GLN VAL THR GLN
SEQRES 3 B 306 LEU LYS GLU GLN VAL PRO GLY PHE THR PRO ARG LEU ALA
SEQRES 4 B 306 ILE LEU GLN VAL GLY ASN ARG ASP ASP SER ASN LEU TYR
SEQRES 5 B 306 ILE ASN VAL LYS LEU LYS ALA ALA GLU GLU ILE GLY ILE
SEQRES 6 B 306 LYS ALA THR HIS ILE LYS LEU PRO ARG THR THR THR GLU
SEQRES 7 B 306 SER GLU VAL MET LYS TYR ILE THR SER LEU ASN GLU ASP
SEQRES 8 B 306 SER THR VAL HIS GLY PHE LEU VAL GLN LEU PRO LEU ASP
SEQRES 9 B 306 SER GLU ASN SER ILE ASN THR GLU GLU VAL ILE ASN ALA
SEQRES 10 B 306 ILE ALA PRO GLU LYS ASP VAL ASP GLY LEU THR SER ILE
SEQRES 11 B 306 ASN ALA GLY ARG LEU ALA ARG GLY ASP LEU ASN ASP CYS
SEQRES 12 B 306 PHE ILE PRO CYS THR PRO LYS GLY CYS LEU GLU LEU ILE
SEQRES 13 B 306 LYS GLU THR GLY VAL PRO ILE ALA GLY ARG HIS ALA VAL
SEQRES 14 B 306 VAL VAL GLY ARG SER LYS ILE VAL GLY ALA PRO MET HIS
SEQRES 15 B 306 ASP LEU LEU LEU TRP ASN ASN ALA THR VAL THR THR CYS
SEQRES 16 B 306 HIS SER LYS THR ALA HIS LEU ASP GLU GLU VAL ASN LYS
SEQRES 17 B 306 GLY ASP ILE LEU VAL VAL ALA THR GLY GLN PRO GLU MET
SEQRES 18 B 306 VAL LYS GLY GLU TRP ILE LYS PRO GLY ALA ILE VAL ILE
SEQRES 19 B 306 ASP CYS GLY ILE ASN TYR VAL PRO ASP ASP LYS LYS PRO
SEQRES 20 B 306 ASN GLY ARG LYS VAL VAL GLY ASP VAL ALA TYR ASP GLU
SEQRES 21 B 306 ALA LYS GLU ARG ALA SER PHE ILE THR PRO VAL PRO GLY
SEQRES 22 B 306 GLY VAL GLY PRO MET THR VAL ALA MET LEU MET GLN SER
SEQRES 23 B 306 THR VAL GLU SER ALA LYS ARG PHE LEU GLU LYS PHE LYS
SEQRES 24 B 306 PRO GLY LYS TRP MET ILE GLN
HET NAP A2001 48
HET L24 A3001 32
HET NAP B2002 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM L24 [[[2-AMINO-5,6,7,8-TETRAHYDRO-4-HYDROXY-PYRIDO[2,3-
HETNAM 2 L24 D]PYRIMIDIN-6-YL]-ETHYL]-PHENYL]-CARBONYL-GLUTAMIC
HETNAM 3 L24 ACID
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN L24 LY249543
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 4 L24 C21 H25 N5 O6
FORMUL 6 HOH *195(H2 O)
HELIX 1 1 ASN A 8 VAL A 31 1 24
HELIX 2 2 ARG A 46 GLY A 64 1 19
HELIX 3 3 THR A 77 ASP A 91 1 15
HELIX 4 4 ASN A 110 ASN A 116 1 7
HELIX 5 5 THR A 128 GLY A 138 1 11
HELIX 6 6 PRO A 146 GLU A 158 1 13
HELIX 7 7 VAL A 177 TRP A 187 1 11
HELIX 8 8 HIS A 201 ASN A 207 1 7
HELIX 9 9 LYS A 223 ILE A 227 5 5
HELIX 10 10 ALA A 257 LYS A 262 1 6
HELIX 11 11 GLY A 274 GLU A 296 1 23
HELIX 12 12 ASN B 1008 VAL B 1031 1 24
HELIX 13 13 ARG B 1046 GLY B 1064 1 19
HELIX 14 14 THR B 1077 ASP B 1091 1 15
HELIX 15 15 ASN B 1110 ASN B 1116 1 7
HELIX 16 16 ALA B 1117 ILE B 1118 5 2
HELIX 17 17 ALA B 1119 LYS B 1122 5 4
HELIX 18 18 THR B 1128 ARG B 1137 1 10
HELIX 19 19 PRO B 1146 GLU B 1158 1 13
HELIX 20 20 VAL B 1177 ASN B 1188 1 12
HELIX 21 21 HIS B 1201 ASN B 1207 1 7
HELIX 22 22 LYS B 1223 ILE B 1227 5 5
HELIX 23 23 ALA B 1257 LYS B 1262 1 6
HELIX 24 24 PRO B 1277 GLU B 1296 1 20
SHEET 1 A12 GLU A 5 ILE A 6 0
SHEET 2 A12 PHE A 267 ILE A 268 1 N ILE A 268 O GLU A 5
SHEET 3 A12 ILE A 232 ASP A 235 1 N VAL A 233 O PHE A 267
SHEET 4 A12 ILE A 211 VAL A 214 1 O LEU A 212 N ILE A 234
SHEET 5 A12 HIS A 167 VAL A 171 1 O HIS A 167 N ILE A 211
SHEET 6 A12 THR A 191 CYS A 195 1 O THR A 191 N ALA A 168
SHEET 7 A12 THR B1191 CYS B1195 -1 O VAL B1192 N THR A 194
SHEET 8 A12 HIS B1167 VAL B1171 1 N ALA B1168 O THR B1191
SHEET 9 A12 ILE B1211 VAL B1214 1 O ILE B1211 N VAL B1169
SHEET 10 A12 ILE B1232 ASP B1235 1 O ILE B1232 N LEU B1212
SHEET 11 A12 PHE B1267 ILE B1268 1 O PHE B1267 N VAL B1233
SHEET 12 A12 GLU B1005 ILE B1006 1 O GLU B1005 N ILE B1268
SHEET 1 B 3 LYS A 66 LEU A 72 0
SHEET 2 B 3 ARG A 37 VAL A 43 1 N LEU A 38 O LYS A 66
SHEET 3 B 3 GLY A 96 VAL A 99 1 O GLY A 96 N ALA A 39
SHEET 1 C 3 LYS B1066 LEU B1072 0
SHEET 2 C 3 ARG B1037 VAL B1043 1 O LEU B1038 N THR B1068
SHEET 3 C 3 GLY B1096 VAL B1099 1 N GLY B1096 O ARG B1037
SHEET 1 D 2 ASN B1239 PRO B1242 0
SHEET 2 D 2 ARG B1250 VAL B1253 -1 N LYS B1251 O VAL B1241
CISPEP 1 LEU A 101 PRO A 102 0 0.05
CISPEP 2 VAL A 271 PRO A 272 0 0.03
CISPEP 3 LEU B 1101 PRO B 1102 0 -0.10
CISPEP 4 VAL B 1271 PRO B 1272 0 0.19
SITE 1 AC1 17 THR A 148 ARG A 173 SER A 174 HIS A 196
SITE 2 AC1 17 SER A 197 LEU A 202 THR A 216 GLY A 217
SITE 3 AC1 17 GLN A 218 MET A 221 CYS A 236 GLY A 237
SITE 4 AC1 17 ILE A 238 GLY A 276 THR A 279 L24 A3001
SITE 5 AC1 17 HOH A4093
SITE 1 AC2 20 THR B1148 ARG B1173 SER B1174 HIS B1196
SITE 2 AC2 20 SER B1197 THR B1216 GLY B1217 GLN B1218
SITE 3 AC2 20 MET B1221 CYS B1236 ILE B1238 GLY B1276
SITE 4 AC2 20 THR B1279 HOH B4018 HOH B4019 HOH B4108
SITE 5 AC2 20 HOH B4109 HOH B4110 HOH B4111 HOH B4185
SITE 1 AC3 11 TYR A 52 VAL A 55 LYS A 56 GLN A 100
SITE 2 AC3 11 LEU A 101 PRO A 272 GLY A 273 PRO A 277
SITE 3 AC3 11 VAL A 280 NAP A2001 HOH A4132
CRYST1 67.871 136.396 61.649 90.00 90.00 90.00 P 21 21 21 8
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 0.014734 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007332 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016221 0.00000
(ATOM LINES ARE NOT SHOWN.)
END