HEADER LIGASE 28-JAN-00 1EE1
TITLE CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS
TITLE 2 SUBTILIS COMPLEXED WITH ONE MOLECULE ATP, TWO MOLECULES DEAMIDO-NAD+
TITLE 3 AND ONE MG2+ ION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NH(3)-DEPENDENT NAD(+) SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NAD(+) SYNTHETASE;
COMPND 5 EC: 6.3.5.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: NADE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LYASE, AMIDOTRANSFERASE, NH3 DEPENDENT, ATP PYROPHOSPHATASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.DEVEDJIEV,J.SYMERSKY,R.SINGH,M.JEDRZEJAS,C.BROUILLETTE,
AUTHOR 2 W.BROUILLETTE,D.MUCCIO,D.CHATTOPADHYAY,L.DELUCAS
REVDAT 5 07-FEB-24 1EE1 1 REMARK LINK
REVDAT 4 04-OCT-17 1EE1 1 REMARK
REVDAT 3 24-FEB-09 1EE1 1 VERSN
REVDAT 2 01-APR-03 1EE1 1 JRNL
REVDAT 1 06-JUN-01 1EE1 0
JRNL AUTH Y.DEVEDJIEV,J.SYMERSKY,R.SINGH,M.JEDRZEJAS,C.BROUILLETTE,
JRNL AUTH 2 W.BROUILLETTE,D.MUCCIO,D.CHATTOPADHYAY,L.DELUCAS
JRNL TITL STABILIZATION OF ACTIVE-SITE LOOPS IN NH3-DEPENDENT NAD+
JRNL TITL 2 SYNTHETASE FROM BACILLUS SUBTILIS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 57 806 2001
JRNL REFN ISSN 0907-4449
JRNL PMID 11375500
JRNL DOI 10.1107/S0907444901003523
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.DEVEDJIEV,R.SINGH,C.BROUILLETTE,D.MUCCIO,W.BROUILLETTE,
REMARK 1 AUTH 2 L.DELUCAS,M.JEDZEJAS
REMARK 1 TITL ASYMMETRIC COMPLEX OF NAD+ SYNTHETASE WITH NATURAL
REMARK 1 TITL 2 SUBSTRATES ATP DEAMIDO-NAD+
REMARK 1 REF AM.CRYST.ASSOC.,ABSTR.PAPERS 1997
REMARK 1 REF 2 (SUMMER MEETING)
REMARK 1 REFN ISSN 0569-4221
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.DEVEDJIEV,R.SINGH,C.BROUILLETTE,D.MUCCIO,W.BROUILLETTE,
REMARK 1 AUTH 2 L.DELUCAS,M.JEDZEJAS
REMARK 1 TITL CATALYTIC CYCLE OF NAD+ SYNTHETASE VIEWED BY X-RAY
REMARK 1 TITL 2 STRUCTURES OF KINETIC INTERMEDIATES
REMARK 1 REF AM.CRYST.ASSOC.,ABSTR.PAPERS 1998
REMARK 1 REF 2 (SUMMER MEETING)
REMARK 1 REFN ISSN 0569-4221
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 23848
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) : 0.154
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1240
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 : 4068
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 120
REMARK 3 SOLVENT ATOMS : 397
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.30
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 2.070
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: USED WEIGHTED LEAST SQUARES PROCEDURE.
REMARK 3
REMARK 3 ALL PORTIONS OF THE BACKBONE IN SUBUNIT A ARE WELL ORDERED.
REMARK 3 HOWEVER, BACKBONE ATOMS AND THE SIDE CHAINS OF RESIDUES
REMARK 3 83-86 AND 205-225 IN SUBUNIT B ARE NOT VISIBLE ON THE
REMARK 3 ELECTRON DENSITY MAP. THE NICOTINIC ACID MOIETY OF
REMARK 3 DEAMIDO-NAD BOUND TO SUBUNIT B IS DISORDERED AS WELL,
REMARK 3 THOUGH THE REMAINDER OF THE SUBSTRATE IS WELL ORDERED.
REMARK 3 COORDINATES OF THE NICOTINIC ACID MOIETY IN SUBUNIT B
REMARK 3 ARE PRESENTED FOR REFERENCE. ATP BINDING SITE IN
REMARK 3 SUBUNIT A IS FULLY OCCUPIED, HOWEVER, NO BINDING OF ATP
REMARK 3 AND MG2+ WAS FOUND IN SUBUNIT B.
REMARK 4
REMARK 4 1EE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010480.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-97
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33464
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.15600
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, SODIUM ACETATE, MAGNESIUM
REMARK 280 CHLORIDE, ADENOSINE TRIPHOSPHATE, DEAMIDO-NAD+, PH 5.2, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 298.0K
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 43.34500
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: 8560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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 THR B 83
REMARK 465 GLN B 84
REMARK 465 GLN B 85
REMARK 465 ASP B 86
REMARK 465 LYS B 205
REMARK 465 GLU B 206
REMARK 465 PRO B 207
REMARK 465 THR B 208
REMARK 465 ALA B 209
REMARK 465 ASP B 210
REMARK 465 LEU B 211
REMARK 465 LEU B 212
REMARK 465 ASP B 213
REMARK 465 GLU B 214
REMARK 465 LYS B 215
REMARK 465 PRO B 216
REMARK 465 GLN B 217
REMARK 465 GLN B 218
REMARK 465 SER B 219
REMARK 465 ASP B 220
REMARK 465 GLU B 221
REMARK 465 THR B 222
REMARK 465 GLU B 223
REMARK 465 LEU B 224
REMARK 465 GLY B 225
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 LEU A 178 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 LEU B 178 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A5500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 208 O
REMARK 620 2 HOH A2381 O 99.1
REMARK 620 3 HOH A2382 O 118.5 120.1
REMARK 620 4 ATP A5000 O2B 136.7 90.8 91.1
REMARK 620 5 ATP A5000 O3G 71.8 75.8 156.3 70.0
REMARK 620 6 ATP A5000 O1A 79.8 150.0 85.1 71.6 75.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 5500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DND A 4000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DND B 3000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 5000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NSY RELATED DB: PDB
REMARK 900 1NSY CONTAINS THE SAME PROTEIN COMPLEXED WITH 2 MOL AMP, TWO PP -
REMARK 900 IONS, TWO MOLECULES ATP AND TWO MG2+ IONS
REMARK 900 RELATED ID: 1IFX RELATED DB: PDB
REMARK 900 ONTAINS THE SAME PROTEIN COMPEXED WITH TWO MOLECULES DEAMIDO-NAD
DBREF 1EE1 A 1 271 UNP P08164 NADE_BACSU 2 272
DBREF 1EE1 B 1 271 UNP P08164 NADE_BACSU 2 272
SEQRES 1 A 271 SER MET GLN GLU LYS ILE MET ARG GLU LEU HIS VAL LYS
SEQRES 2 A 271 PRO SER ILE ASP PRO LYS GLN GLU ILE GLU ASP ARG VAL
SEQRES 3 A 271 ASN PHE LEU LYS GLN TYR VAL LYS LYS THR GLY ALA LYS
SEQRES 4 A 271 GLY PHE VAL LEU GLY ILE SER GLY GLY GLN ASP SER THR
SEQRES 5 A 271 LEU ALA GLY ARG LEU ALA GLN LEU ALA VAL GLU SER ILE
SEQRES 6 A 271 ARG GLU GLU GLY GLY ASP ALA GLN PHE ILE ALA VAL ARG
SEQRES 7 A 271 LEU PRO HIS GLY THR GLN GLN ASP GLU ASP ASP ALA GLN
SEQRES 8 A 271 LEU ALA LEU LYS PHE ILE LYS PRO ASP LYS SER TRP LYS
SEQRES 9 A 271 PHE ASP ILE LYS SER THR VAL SER ALA PHE SER ASP GLN
SEQRES 10 A 271 TYR GLN GLN GLU THR GLY ASP GLN LEU THR ASP PHE ASN
SEQRES 11 A 271 LYS GLY ASN VAL LYS ALA ARG THR ARG MET ILE ALA GLN
SEQRES 12 A 271 TYR ALA ILE GLY GLY GLN GLU GLY LEU LEU VAL LEU GLY
SEQRES 13 A 271 THR ASP HIS ALA ALA GLU ALA VAL THR GLY PHE PHE THR
SEQRES 14 A 271 LYS TYR GLY ASP GLY GLY ALA ASP LEU LEU PRO LEU THR
SEQRES 15 A 271 GLY LEU THR LYS ARG GLN GLY ARG THR LEU LEU LYS GLU
SEQRES 16 A 271 LEU GLY ALA PRO GLU ARG LEU TYR LEU LYS GLU PRO THR
SEQRES 17 A 271 ALA ASP LEU LEU ASP GLU LYS PRO GLN GLN SER ASP GLU
SEQRES 18 A 271 THR GLU LEU GLY ILE SER TYR ASP GLU ILE ASP ASP TYR
SEQRES 19 A 271 LEU GLU GLY LYS GLU VAL SER ALA LYS VAL SER GLU ALA
SEQRES 20 A 271 LEU GLU LYS ARG TYR SER MET THR GLU HIS LYS ARG GLN
SEQRES 21 A 271 VAL PRO ALA SER MET PHE ASP ASP TRP TRP LYS
SEQRES 1 B 271 SER MET GLN GLU LYS ILE MET ARG GLU LEU HIS VAL LYS
SEQRES 2 B 271 PRO SER ILE ASP PRO LYS GLN GLU ILE GLU ASP ARG VAL
SEQRES 3 B 271 ASN PHE LEU LYS GLN TYR VAL LYS LYS THR GLY ALA LYS
SEQRES 4 B 271 GLY PHE VAL LEU GLY ILE SER GLY GLY GLN ASP SER THR
SEQRES 5 B 271 LEU ALA GLY ARG LEU ALA GLN LEU ALA VAL GLU SER ILE
SEQRES 6 B 271 ARG GLU GLU GLY GLY ASP ALA GLN PHE ILE ALA VAL ARG
SEQRES 7 B 271 LEU PRO HIS GLY THR GLN GLN ASP GLU ASP ASP ALA GLN
SEQRES 8 B 271 LEU ALA LEU LYS PHE ILE LYS PRO ASP LYS SER TRP LYS
SEQRES 9 B 271 PHE ASP ILE LYS SER THR VAL SER ALA PHE SER ASP GLN
SEQRES 10 B 271 TYR GLN GLN GLU THR GLY ASP GLN LEU THR ASP PHE ASN
SEQRES 11 B 271 LYS GLY ASN VAL LYS ALA ARG THR ARG MET ILE ALA GLN
SEQRES 12 B 271 TYR ALA ILE GLY GLY GLN GLU GLY LEU LEU VAL LEU GLY
SEQRES 13 B 271 THR ASP HIS ALA ALA GLU ALA VAL THR GLY PHE PHE THR
SEQRES 14 B 271 LYS TYR GLY ASP GLY GLY ALA ASP LEU LEU PRO LEU THR
SEQRES 15 B 271 GLY LEU THR LYS ARG GLN GLY ARG THR LEU LEU LYS GLU
SEQRES 16 B 271 LEU GLY ALA PRO GLU ARG LEU TYR LEU LYS GLU PRO THR
SEQRES 17 B 271 ALA ASP LEU LEU ASP GLU LYS PRO GLN GLN SER ASP GLU
SEQRES 18 B 271 THR GLU LEU GLY ILE SER TYR ASP GLU ILE ASP ASP TYR
SEQRES 19 B 271 LEU GLU GLY LYS GLU VAL SER ALA LYS VAL SER GLU ALA
SEQRES 20 B 271 LEU GLU LYS ARG TYR SER MET THR GLU HIS LYS ARG GLN
SEQRES 21 B 271 VAL PRO ALA SER MET PHE ASP ASP TRP TRP LYS
HET MG A5500 1
HET DND A4000 44
HET ATP A5000 31
HET DND B3000 44
HETNAM MG MAGNESIUM ION
HETNAM DND NICOTINIC ACID ADENINE DINUCLEOTIDE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETSYN DND DEAMIDO-NAD+
FORMUL 3 MG MG 2+
FORMUL 4 DND 2(C21 H27 N6 O15 P2 1+)
FORMUL 5 ATP C10 H16 N5 O13 P3
FORMUL 7 HOH *397(H2 O)
HELIX 1 1 MET A 2 LEU A 10 1 9
HELIX 2 2 PRO A 18 THR A 36 1 19
HELIX 3 3 GLN A 49 GLU A 68 1 20
HELIX 4 4 GLU A 87 ILE A 97 1 11
HELIX 5 5 LYS A 108 THR A 122 1 15
HELIX 6 6 ASP A 128 GLU A 150 1 23
HELIX 7 7 ALA A 160 ALA A 163 1 4
HELIX 8 8 LYS A 186 LEU A 196 1 11
HELIX 9 9 GLU A 200 LEU A 204 1 5
HELIX 10 10 ASP A 220 LEU A 224 1 5
HELIX 11 11 TYR A 228 LEU A 235 1 8
HELIX 12 12 ALA A 242 ARG A 259 1 18
HELIX 13 13 MET B 2 GLU B 9 1 8
HELIX 14 14 PRO B 18 THR B 36 1 19
HELIX 15 15 GLN B 49 GLU B 67 1 19
HELIX 16 16 GLU B 87 ILE B 97 1 11
HELIX 17 17 LYS B 108 THR B 122 1 15
HELIX 18 18 ASP B 128 GLU B 150 1 23
HELIX 19 19 ALA B 160 ALA B 163 1 4
HELIX 20 20 LYS B 186 GLU B 195 1 10
HELIX 21 21 GLU B 200 TYR B 203 1 4
HELIX 22 23 TYR B 228 LEU B 235 1 8
HELIX 23 24 ALA B 242 ARG B 259 1 18
SHEET 1 A 3 GLY A 40 GLY A 44 0
SHEET 2 A 3 GLN A 73 ARG A 78 1 N GLN A 73 O PHE A 41
SHEET 3 A 3 LYS A 101 LYS A 104 1 N LYS A 101 O ALA A 76
SHEET 1 B 3 GLY B 40 GLY B 44 0
SHEET 2 B 3 GLN B 73 ARG B 78 1 N GLN B 73 O PHE B 41
SHEET 3 B 3 LYS B 101 LYS B 104 1 N LYS B 101 O ALA B 76
LINK O THR A 208 MG MG A5500 1555 1555 1.92
LINK O HOH A2381 MG MG A5500 1555 1555 1.72
LINK O HOH A2382 MG MG A5500 1555 1555 1.63
LINK O2B ATP A5000 MG MG A5500 1555 1555 2.28
LINK O3G ATP A5000 MG MG A5500 1555 1555 2.78
LINK O1A ATP A5000 MG MG A5500 1555 1555 2.33
SITE 1 AC1 4 THR A 208 HOH A2381 HOH A2382 ATP A5000
SITE 1 AC2 27 PHE A 129 ASN A 133 ARG A 137 PHE A 167
SITE 2 AC2 27 PHE A 168 THR A 169 LYS A 170 ASP A 173
SITE 3 AC2 27 ALA A 209 LEU A 211 GLU A 223 HIS A 257
SITE 4 AC2 27 LYS A 258 HOH A2101 HOH A2158 HOH A2206
SITE 5 AC2 27 HOH A2213 HOH A2223 HOH A2238 HOH A2284
SITE 6 AC2 27 ATP A5000 TYR B 32 THR B 36 TYR B 144
SITE 7 AC2 27 LEU B 153 ASP B 177 HOH B2071
SITE 1 AC3 22 TYR A 32 THR A 36 TYR A 144 LEU A 153
SITE 2 AC3 22 ASP A 177 HOH A2027 PHE B 129 ASN B 133
SITE 3 AC3 22 ARG B 137 PHE B 167 PHE B 168 THR B 169
SITE 4 AC3 22 LYS B 170 ASP B 173 HIS B 257 LYS B 258
SITE 5 AC3 22 HOH B2127 HOH B2228 HOH B2270 HOH B2304
SITE 6 AC3 22 HOH B2372 HOH B2377
SITE 1 AC4 28 LEU A 43 GLY A 44 ILE A 45 SER A 46
SITE 2 AC4 28 GLY A 48 ASP A 50 SER A 51 ARG A 78
SITE 3 AC4 28 LEU A 79 GLN A 84 ARG A 139 THR A 157
SITE 4 AC4 28 ASP A 173 LYS A 186 PRO A 207 THR A 208
SITE 5 AC4 28 HOH A2012 HOH A2019 HOH A2023 HOH A2062
SITE 6 AC4 28 HOH A2080 HOH A2238 HOH A2284 HOH A2326
SITE 7 AC4 28 HOH A2381 HOH A2382 DND A4000 MG A5500
CRYST1 52.980 86.690 60.480 90.00 111.18 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 0.018875 0.000000 0.007313 0.00000
SCALE2 0.000000 0.011535 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017732 0.00000
(ATOM LINES ARE NOT SHOWN.)
END