HEADER OXIDOREDUCTASE 01-APR-99 1CIV
TITLE CHLOROPLAST NADP-DEPENDENT MALATE DEHYDROGENASE FROM FLAVERIA BIDENTIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NADP-MALATE DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.82
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FLAVERIA BIDENTIS;
SOURCE 3 ORGANISM_TAXID: 4224;
SOURCE 4 ORGAN: LEAF;
SOURCE 5 ORGANELLE: CHLOROPLAST;
SOURCE 6 OTHER_DETAILS: DARKENED LEAVES
KEYWDS CHLOROPLAST, LIGHT ACTIVATED, NADP-DEPENDENT, DEHYDROGENASE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.D.CARR,A.R.ASHTON,D.VERGER,D.L.OLLIS
REVDAT 7 09-AUG-23 1CIV 1 REMARK
REVDAT 6 20-NOV-19 1CIV 1 JRNL
REVDAT 5 11-APR-18 1CIV 1 REMARK
REVDAT 4 04-APR-18 1CIV 1 REMARK
REVDAT 3 13-JUL-11 1CIV 1 VERSN
REVDAT 2 24-FEB-09 1CIV 1 VERSN
REVDAT 1 05-APR-00 1CIV 0
JRNL AUTH P.D.CARR,D.VERGER,A.R.ASHTON,D.L.OLLIS
JRNL TITL CHLOROPLAST NADP-MALATE DEHYDROGENASE: STRUCTURAL BASIS OF
JRNL TITL 2 LIGHT-DEPENDENT REGULATION OF ACTIVITY BY THIOL OXIDATION
JRNL TITL 3 AND REDUCTION.
JRNL REF STRUCTURE FOLD.DES. V. 7 461 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10196131
JRNL DOI 10.1016/S0969-2126(99)80058-6
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.H.MACPHERSON,A.R.ASHTON,P.D.CARR,S.J.TREVANION,D.VERGER,
REMARK 1 AUTH 2 D.L.OLLIS
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDIES OF
REMARK 1 TITL 2 CHLOROPLAST NADP-DEPENDENT MALATE DEHYDROGENASE FROM
REMARK 1 TITL 3 FLAVERIA BIDENTIS.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 54 654 1998
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 9761865
REMARK 1 DOI 10.1107/S0907444997015655
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.84
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 250.000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.8
REMARK 3 NUMBER OF REFLECTIONS : 17473
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : R-FREE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.78
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.88
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.81
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1096
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 54
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 : 2805
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 106
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) : 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) : 15.0
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.740
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 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM.NADP
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOP.NADP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CIV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000787.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-96
REMARK 200 TEMPERATURE (KELVIN) : 100.00
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20335
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.13200
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: 4MDH
REMARK 200
REMARK 200 REMARK: BOTH SIRAS AND MOLECULAR REPLACEMENT METHODS WERE USED
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE MACPHERSON ET AL. (1998) ACTA
REMARK 280 CRYST, D54, 654 - 656, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.26667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 21.63333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 21.63333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 43.26667
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 255.99711
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 86.53333
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 SER A 1
REMARK 465 VAL A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 SER A 5
REMARK 465 ASP A 6
REMARK 465 GLN A 7
REMARK 465 ILE A 8
REMARK 465 GLN A 9
REMARK 465 ALA A 10
REMARK 465 PRO A 11
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 GLN A 16 CG CD OE1 NE2
REMARK 470 LYS A 17 CG CD CE NZ
REMARK 470 GLU A 19 CG CD OE1 OE2
REMARK 470 TYR A 28 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 30 CG CD1 CD2
REMARK 470 LYS A 31 CG CD CE NZ
REMARK 470 GLU A 33 CG CD OE1 OE2
REMARK 470 GLU A 34 CG CD OE1 OE2
REMARK 470 GLU A 35 CG CD OE1 OE2
REMARK 470 THR A 36 OG1 CG2
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 LYS A 41 CG CD CE NZ
REMARK 470 ARG A 83 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 130 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 215 CG CD CE NZ
REMARK 470 LYS A 270 CG CD CE NZ
REMARK 470 LYS A 327 CG CD CE NZ
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 A 273 N - CA - C ANGL. DEV. = 18.4 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 LYS A 15 -15.04 80.28
REMARK 500 VAL A 23 -38.90 116.63
REMARK 500 TYR A 28 -157.96 -57.80
REMARK 500 ASP A 29 -88.62 -70.77
REMARK 500 LEU A 30 108.06 -172.19
REMARK 500 LYS A 31 -45.92 -11.96
REMARK 500 ALA A 32 -3.13 -59.40
REMARK 500 GLU A 34 -71.32 -105.98
REMARK 500 PRO A 160 -15.03 -46.19
REMARK 500 THR A 227 10.29 -64.48
REMARK 500 PRO A 231 96.47 -69.58
REMARK 500 HIS A 239 -7.49 61.13
REMARK 500 TRP A 272 112.64 23.75
REMARK 500 SER A 276 46.13 -75.62
REMARK 500 GLU A 377 28.68 -72.70
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 386
DBREF 1CIV A 1 385 UNP P46489 MDHP_FLABI 69 453
SEQRES 1 A 385 SER VAL THR SER SER ASP GLN ILE GLN ALA PRO LEU PRO
SEQRES 2 A 385 ALA LYS GLN LYS PRO GLU CYS PHE GLY VAL PHE CYS LEU
SEQRES 3 A 385 THR TYR ASP LEU LYS ALA GLU GLU GLU THR LYS SER TRP
SEQRES 4 A 385 LYS LYS ILE ILE ASN VAL ALA VAL SER GLY ALA ALA GLY
SEQRES 5 A 385 MET ILE SER ASN HIS LEU LEU PHE LYS LEU ALA SER GLY
SEQRES 6 A 385 GLU VAL PHE GLY PRO ASP GLN PRO ILE SER LEU LYS LEU
SEQRES 7 A 385 LEU GLY SER GLU ARG SER PHE ALA ALA LEU GLU GLY VAL
SEQRES 8 A 385 ALA MET GLU LEU GLU ASP SER LEU TYR PRO LEU LEU ARG
SEQRES 9 A 385 GLN VAL SER ILE GLY ILE ASP PRO TYR GLU ILE PHE GLN
SEQRES 10 A 385 ASP ALA GLU TRP ALA LEU LEU ILE GLY ALA LYS PRO ARG
SEQRES 11 A 385 GLY PRO GLY MET GLU ARG ALA ASP LEU LEU ASP ILE ASN
SEQRES 12 A 385 GLY GLN ILE PHE ALA GLU GLN GLY LYS ALA LEU ASN ALA
SEQRES 13 A 385 VAL ALA SER PRO ASN VAL LYS VAL MET VAL VAL GLY ASN
SEQRES 14 A 385 PRO CYS ASN THR ASN ALA LEU ILE CYS LEU LYS ASN ALA
SEQRES 15 A 385 PRO ASN ILE PRO PRO LYS ASN PHE HIS ALA LEU THR ARG
SEQRES 16 A 385 LEU ASP GLU ASN ARG ALA LYS CYS GLN LEU ALA LEU LYS
SEQRES 17 A 385 ALA GLY VAL PHE TYR ASP LYS VAL SER ASN VAL THR ILE
SEQRES 18 A 385 TRP GLY ASN HIS SER THR THR GLN VAL PRO ASP PHE LEU
SEQRES 19 A 385 ASN ALA LYS ILE HIS GLY ILE PRO VAL THR GLU VAL ILE
SEQRES 20 A 385 ARG ASP ARG LYS TRP LEU GLU ASP GLU PHE THR ASN MET
SEQRES 21 A 385 VAL GLN THR ARG GLY GLY VAL LEU ILE LYS LYS TRP GLY
SEQRES 22 A 385 ARG SER SER ALA ALA SER THR ALA VAL SER ILE VAL ASP
SEQRES 23 A 385 ALA ILE ARG SER LEU VAL THR PRO THR PRO GLU GLY ASP
SEQRES 24 A 385 TRP PHE SER THR GLY VAL TYR THR ASN GLY ASN PRO TYR
SEQRES 25 A 385 GLY ILE ALA GLU ASP ILE VAL PHE SER MET PRO CYS ARG
SEQRES 26 A 385 SER LYS GLY ASP GLY ASP TYR GLU PHE VAL LYS ASP VAL
SEQRES 27 A 385 ILE PHE ASP ASP TYR LEU SER LYS LYS ILE LYS LYS SER
SEQRES 28 A 385 GLU ASP GLU LEU LEU ALA GLU LYS LYS CYS VAL ALA HIS
SEQRES 29 A 385 LEU THR GLY GLU GLY ILE ALA VAL CYS ASP LEU PRO GLU
SEQRES 30 A 385 ASP THR MET LEU PRO GLY GLU MET
HET NAP A 386 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 HOH *106(H2 O)
HELIX 1 1 MET A 53 ALA A 63 1 11
HELIX 2 2 GLU A 82 SER A 98 5 17
HELIX 3 3 PRO A 112 ILE A 115 1 4
HELIX 4 4 ARG A 136 VAL A 157 1 22
HELIX 5 5 CYS A 171 ASN A 181 1 11
HELIX 6 6 PRO A 187 ASN A 189 5 3
HELIX 7 7 ARG A 195 ALA A 209 1 15
HELIX 8 8 VAL A 243 GLU A 245 5 3
HELIX 9 9 ARG A 250 ASP A 255 1 6
HELIX 10 10 PHE A 257 LYS A 270 1 14
HELIX 11 11 ALA A 277 VAL A 292 1 16
HELIX 12 12 ASP A 342 THR A 366 1 25
SHEET 1 A 6 PHE A 190 ALA A 192 0
SHEET 2 A 6 LYS A 163 VAL A 166 1 N VAL A 164 O HIS A 191
SHEET 3 A 6 TRP A 121 LEU A 124 1 N ALA A 122 O LYS A 163
SHEET 4 A 6 ILE A 43 SER A 48 1 N ALA A 46 O TRP A 121
SHEET 5 A 6 ILE A 74 LEU A 79 1 N SER A 75 O ILE A 43
SHEET 6 A 6 LEU A 103 GLY A 109 1 N ARG A 104 O ILE A 74
SHEET 1 B 2 THR A 220 TRP A 222 0
SHEET 2 B 2 VAL A 230 ASP A 232 -1 N ASP A 232 O THR A 220
SHEET 1 C 2 PHE A 301 TYR A 306 0
SHEET 2 C 2 VAL A 319 CYS A 324 -1 N CYS A 324 O PHE A 301
SSBOND 1 CYS A 20 CYS A 25 1555 1555 2.03
SSBOND 2 CYS A 361 CYS A 373 1555 1555 2.03
CISPEP 1 ASN A 169 PRO A 170 0 0.52
SITE 1 AC1 27 GLY A 49 ALA A 50 ALA A 51 GLY A 52
SITE 2 AC1 27 MET A 53 ILE A 54 GLY A 80 SER A 81
SITE 3 AC1 27 SER A 84 ALA A 127 GLN A 150 VAL A 167
SITE 4 AC1 27 GLY A 168 ASN A 169 LEU A 193 HIS A 225
SITE 5 AC1 27 THR A 280 MET A 380 GLU A 384 MET A 385
SITE 6 AC1 27 HOH A 387 HOH A 393 HOH A 394 HOH A 399
SITE 7 AC1 27 HOH A 431 HOH A 440 HOH A 533
CRYST1 147.800 147.800 64.900 90.00 90.00 120.00 P 32 2 1 6
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 0.006766 0.003906 0.000000 0.00000
SCALE2 0.000000 0.007812 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015408 0.00000
(ATOM LINES ARE NOT SHOWN.)
END