HEADER TRANSFERASE 24-NOV-04 1Y3H
TITLE CRYSTAL STRUCTURE OF INORGANIC POLYPHOSPHATE/ATP-NAD KINASE FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INORGANIC POLYPHOSPHATE/ATP-NAD KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: POLY(P)/ATP NAD KINASE;
COMPND 5 EC: 2.7.1.23;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: PPNK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSK27
KEYWDS NAD KINASE, POLYPHOSPHATE, NAD, ATP, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MORI,M.YAMASAKI,Y.MARUYAMA,K.MOMMA,S.KAWAI,W.HASHIMOTO,B.MIKAMI,
AUTHOR 2 K.MURATA
REVDAT 3 10-NOV-21 1Y3H 1 SEQADV
REVDAT 2 24-FEB-09 1Y3H 1 VERSN
REVDAT 1 18-JAN-05 1Y3H 0
JRNL AUTH S.MORI,M.YAMASAKI,Y.MARUYAMA,K.MOMMA,S.KAWAI,W.HASHIMOTO,
JRNL AUTH 2 B.MIKAMI,K.MURATA
JRNL TITL NAD-BINDING MODE AND THE SIGNIFICANCE OF INTERSUBUNIT
JRNL TITL 2 CONTACT REVEALED BY THE CRYSTAL STRUCTURE OF MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS NAD KINASE-NAD COMPLEX
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 327 500 2005
JRNL REFN ISSN 0006-291X
JRNL PMID 15629142
JRNL DOI 10.1016/J.BBRC.2004.11.163
REMARK 2
REMARK 2 RESOLUTION. 2.80 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1056320.370
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 79.4
REMARK 3 NUMBER OF REFLECTIONS : 15057
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) : 0.221
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 716
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 53.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1575
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 91
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.033
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4043
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 27
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -13.63000
REMARK 3 B22 (A**2) : 16.48000
REMARK 3 B33 (A**2) : -2.85000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.52000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM SIGMAA (A) : 0.58
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.58
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
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) : 1.420 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.520 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.670 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.740 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 47.50
REMARK 3
REMARK 3 NCS MODEL : CONSTR
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 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
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 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Y3H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031068.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 6.0
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 : MACSCIENCE
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 : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS HI-STAR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SADIE
REMARK 200 DATA SCALING SOFTWARE : SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18419
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.4
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: MIR
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM 2
REMARK 280 -MORPHOLINOETHANESULFONIC ACID, PH 6.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 70.08800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.72150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.08800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.72150
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: THE BIOLOGICAL UNIT IS A TETRAMER
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: TETRAMERIC
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 2.52478
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 162.37018
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 THR A 2
REMARK 465 ALA A 3
REMARK 465 HIS A 4
REMARK 465 GLY A 14
REMARK 465 ARG A 15
REMARK 465 ASP A 16
REMARK 465 GLU A 17
REMARK 465 ALA A 18
REMARK 465 ALA A 41
REMARK 465 GLU A 42
REMARK 465 ALA A 43
REMARK 465 VAL A 44
REMARK 465 ASP A 45
REMARK 465 ARG A 46
REMARK 465 GLY A 47
REMARK 465 SER A 48
REMARK 465 LEU A 49
REMARK 465 HIS A 50
REMARK 465 LEU A 51
REMARK 465 ALA A 52
REMARK 465 PRO A 53
REMARK 465 ASP A 54
REMARK 465 ASP A 55
REMARK 465 MET A 56
REMARK 465 ARG A 57
REMARK 465 ALA A 58
REMARK 465 MET A 59
REMARK 465 GLY A 60
REMARK 465 VAL A 61
REMARK 465 GLU A 62
REMARK 465 ILE A 63
REMARK 465 GLU A 64
REMARK 465 VAL A 65
REMARK 465 VAL A 66
REMARK 465 ASP A 67
REMARK 465 ALA A 68
REMARK 465 ASP A 69
REMARK 465 GLN A 70
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 HIS B 4
REMARK 465 GLY B 14
REMARK 465 ARG B 15
REMARK 465 ASP B 16
REMARK 465 GLU B 17
REMARK 465 ALA B 18
REMARK 465 THR B 19
REMARK 465 ALA B 41
REMARK 465 GLU B 42
REMARK 465 ALA B 43
REMARK 465 VAL B 44
REMARK 465 ASP B 45
REMARK 465 ARG B 46
REMARK 465 GLY B 47
REMARK 465 SER B 48
REMARK 465 LEU B 49
REMARK 465 HIS B 50
REMARK 465 LEU B 51
REMARK 465 ALA B 52
REMARK 465 PRO B 53
REMARK 465 ASP B 54
REMARK 465 ASP B 55
REMARK 465 MET B 56
REMARK 465 ARG B 57
REMARK 465 ALA B 58
REMARK 465 MET B 59
REMARK 465 GLY B 60
REMARK 465 VAL B 61
REMARK 465 GLU B 62
REMARK 465 ILE B 63
REMARK 465 GLU B 64
REMARK 465 VAL B 65
REMARK 465 VAL B 66
REMARK 465 ASP B 67
REMARK 465 ALA B 68
REMARK 465 ASP B 69
REMARK 465 GLN B 70
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 PRO B 213 C - N - CA ANGL. DEV. = 10.3 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 HIS A 12 -95.07 -51.73
REMARK 500 ALA A 35 158.33 -47.11
REMARK 500 ALA A 72 89.18 -44.12
REMARK 500 ASP A 74 -164.88 -73.40
REMARK 500 CYS A 76 -173.52 -56.64
REMARK 500 PRO A 101 153.72 -46.21
REMARK 500 LEU A 107 -78.98 -118.63
REMARK 500 ARG A 109 -161.77 -67.22
REMARK 500 ALA A 120 12.24 -147.83
REMARK 500 ILE A 121 -32.85 -38.98
REMARK 500 ASN A 159 -58.26 -128.55
REMARK 500 CYS A 188 -173.00 -171.73
REMARK 500 ALA A 201 -135.17 -64.92
REMARK 500 ALA A 217 -169.62 -165.86
REMARK 500 HIS A 226 67.31 -117.02
REMARK 500 ASP A 248 59.84 -92.37
REMARK 500 HIS A 250 -173.99 -64.79
REMARK 500 ARG A 259 -83.13 -85.60
REMARK 500 MET A 262 115.00 172.57
REMARK 500 ALA A 266 146.16 -34.44
REMARK 500 ASP A 285 97.51 -51.16
REMARK 500 ARG A 295 -82.12 -54.91
REMARK 500 LYS A 296 -35.83 -35.18
REMARK 500 ARG A 298 76.73 59.73
REMARK 500 ARG A 305 -62.70 -104.31
REMARK 500 THR B 21 2.14 -65.94
REMARK 500 LYS B 33 70.43 43.55
REMARK 500 ALA B 72 88.12 -46.35
REMARK 500 CYS B 76 173.69 -42.50
REMARK 500 SER B 99 47.97 84.06
REMARK 500 ILE B 151 91.01 -53.50
REMARK 500 VAL B 193 89.20 -150.91
REMARK 500 ALA B 201 -120.99 -84.77
REMARK 500 ALA B 206 1.04 -67.11
REMARK 500 HIS B 250 -167.59 -79.47
REMARK 500 ASP B 257 17.87 47.43
REMARK 500 ARG B 259 -66.66 -131.15
REMARK 500 ASP B 285 102.05 -35.51
REMARK 500 ARG B 298 32.03 70.85
REMARK 500 ARG B 305 -78.24 -94.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y3I RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, NAD COMPLEX
DBREF 1Y3H A 1 307 UNP P0A5S6 PPNK_MYCTU 1 307
DBREF 1Y3H B 1 307 UNP P0A5S6 PPNK_MYCTU 1 307
SEQADV 1Y3H ILE A 302 UNP P0A5S6 THR 302 ENGINEERED MUTATION
SEQADV 1Y3H ILE B 302 UNP P0A5S6 THR 302 ENGINEERED MUTATION
SEQRES 1 A 307 MET THR ALA HIS ARG SER VAL LEU LEU VAL VAL HIS THR
SEQRES 2 A 307 GLY ARG ASP GLU ALA THR GLU THR ALA ARG ARG VAL GLU
SEQRES 3 A 307 LYS VAL LEU GLY ASP ASN LYS ILE ALA LEU ARG VAL LEU
SEQRES 4 A 307 SER ALA GLU ALA VAL ASP ARG GLY SER LEU HIS LEU ALA
SEQRES 5 A 307 PRO ASP ASP MET ARG ALA MET GLY VAL GLU ILE GLU VAL
SEQRES 6 A 307 VAL ASP ALA ASP GLN HIS ALA ALA ASP GLY CYS GLU LEU
SEQRES 7 A 307 VAL LEU VAL LEU GLY GLY ASP GLY THR PHE LEU ARG ALA
SEQRES 8 A 307 ALA GLU LEU ALA ARG ASN ALA SER ILE PRO VAL LEU GLY
SEQRES 9 A 307 VAL ASN LEU GLY ARG ILE GLY PHE LEU ALA GLU ALA GLU
SEQRES 10 A 307 ALA GLU ALA ILE ASP ALA VAL LEU GLU HIS VAL VAL ALA
SEQRES 11 A 307 GLN ASP TYR ARG VAL GLU ASP ARG LEU THR LEU ASP VAL
SEQRES 12 A 307 VAL VAL ARG GLN GLY GLY ARG ILE VAL ASN ARG GLY TRP
SEQRES 13 A 307 ALA LEU ASN GLU VAL SER LEU GLU LYS GLY PRO ARG LEU
SEQRES 14 A 307 GLY VAL LEU GLY VAL VAL VAL GLU ILE ASP GLY ARG PRO
SEQRES 15 A 307 VAL SER ALA PHE GLY CYS ASP GLY VAL LEU VAL SER THR
SEQRES 16 A 307 PRO THR GLY SER THR ALA TYR ALA PHE SER ALA GLY GLY
SEQRES 17 A 307 PRO VAL LEU TRP PRO ASP LEU GLU ALA ILE LEU VAL VAL
SEQRES 18 A 307 PRO ASN ASN ALA HIS ALA LEU PHE GLY ARG PRO MET VAL
SEQRES 19 A 307 THR SER PRO GLU ALA THR ILE ALA ILE GLU ILE GLU ALA
SEQRES 20 A 307 ASP GLY HIS ASP ALA LEU VAL PHE CYS ASP GLY ARG ARG
SEQRES 21 A 307 GLU MET LEU ILE PRO ALA GLY SER ARG LEU GLU VAL THR
SEQRES 22 A 307 ARG CYS VAL THR SER VAL LYS TRP ALA ARG LEU ASP SER
SEQRES 23 A 307 ALA PRO PHE THR ASP ARG LEU VAL ARG LYS PHE ARG LEU
SEQRES 24 A 307 PRO VAL ILE GLY TRP ARG GLY LYS
SEQRES 1 B 307 MET THR ALA HIS ARG SER VAL LEU LEU VAL VAL HIS THR
SEQRES 2 B 307 GLY ARG ASP GLU ALA THR GLU THR ALA ARG ARG VAL GLU
SEQRES 3 B 307 LYS VAL LEU GLY ASP ASN LYS ILE ALA LEU ARG VAL LEU
SEQRES 4 B 307 SER ALA GLU ALA VAL ASP ARG GLY SER LEU HIS LEU ALA
SEQRES 5 B 307 PRO ASP ASP MET ARG ALA MET GLY VAL GLU ILE GLU VAL
SEQRES 6 B 307 VAL ASP ALA ASP GLN HIS ALA ALA ASP GLY CYS GLU LEU
SEQRES 7 B 307 VAL LEU VAL LEU GLY GLY ASP GLY THR PHE LEU ARG ALA
SEQRES 8 B 307 ALA GLU LEU ALA ARG ASN ALA SER ILE PRO VAL LEU GLY
SEQRES 9 B 307 VAL ASN LEU GLY ARG ILE GLY PHE LEU ALA GLU ALA GLU
SEQRES 10 B 307 ALA GLU ALA ILE ASP ALA VAL LEU GLU HIS VAL VAL ALA
SEQRES 11 B 307 GLN ASP TYR ARG VAL GLU ASP ARG LEU THR LEU ASP VAL
SEQRES 12 B 307 VAL VAL ARG GLN GLY GLY ARG ILE VAL ASN ARG GLY TRP
SEQRES 13 B 307 ALA LEU ASN GLU VAL SER LEU GLU LYS GLY PRO ARG LEU
SEQRES 14 B 307 GLY VAL LEU GLY VAL VAL VAL GLU ILE ASP GLY ARG PRO
SEQRES 15 B 307 VAL SER ALA PHE GLY CYS ASP GLY VAL LEU VAL SER THR
SEQRES 16 B 307 PRO THR GLY SER THR ALA TYR ALA PHE SER ALA GLY GLY
SEQRES 17 B 307 PRO VAL LEU TRP PRO ASP LEU GLU ALA ILE LEU VAL VAL
SEQRES 18 B 307 PRO ASN ASN ALA HIS ALA LEU PHE GLY ARG PRO MET VAL
SEQRES 19 B 307 THR SER PRO GLU ALA THR ILE ALA ILE GLU ILE GLU ALA
SEQRES 20 B 307 ASP GLY HIS ASP ALA LEU VAL PHE CYS ASP GLY ARG ARG
SEQRES 21 B 307 GLU MET LEU ILE PRO ALA GLY SER ARG LEU GLU VAL THR
SEQRES 22 B 307 ARG CYS VAL THR SER VAL LYS TRP ALA ARG LEU ASP SER
SEQRES 23 B 307 ALA PRO PHE THR ASP ARG LEU VAL ARG LYS PHE ARG LEU
SEQRES 24 B 307 PRO VAL ILE GLY TRP ARG GLY LYS
FORMUL 3 HOH *27(H2 O)
HELIX 1 1 THR A 21 ASP A 31 1 11
HELIX 2 2 GLY A 84 SER A 99 1 16
HELIX 3 3 GLU A 117 GLU A 119 5 3
HELIX 4 4 ALA A 120 GLN A 131 1 12
HELIX 5 5 PRO A 196 SER A 199 5 4
HELIX 6 6 ALA A 201 GLY A 207 1 7
HELIX 7 7 PRO A 288 ARG A 298 1 11
HELIX 8 8 THR B 21 ASN B 32 1 12
HELIX 9 9 GLY B 84 SER B 99 1 16
HELIX 10 10 ALA B 120 GLN B 131 1 12
HELIX 11 11 THR B 197 THR B 200 5 4
HELIX 12 12 ALA B 201 ALA B 206 1 6
HELIX 13 13 PRO B 288 ARG B 298 1 11
SHEET 1 A 4 LEU A 36 LEU A 39 0
SHEET 2 A 4 VAL A 7 VAL A 11 1 N VAL A 11 O LEU A 39
SHEET 3 A 4 VAL A 79 GLY A 83 1 O LEU A 82 N VAL A 10
SHEET 4 A 4 VAL A 102 ASN A 106 1 O VAL A 105 N GLY A 83
SHEET 1 B 2 ARG A 134 ARG A 138 0
SHEET 2 B 2 VAL A 279 ARG A 283 -1 O ARG A 283 N ARG A 134
SHEET 1 C 6 ARG A 150 ALA A 157 0
SHEET 2 C 6 LEU A 141 GLN A 147 -1 N LEU A 141 O ALA A 157
SHEET 3 C 6 ARG A 269 ARG A 274 -1 O GLU A 271 N VAL A 144
SHEET 4 C 6 ILE A 241 ILE A 245 -1 N ILE A 241 O VAL A 272
SHEET 5 C 6 LEU A 172 ILE A 178 -1 N VAL A 175 O GLU A 244
SHEET 6 C 6 ARG A 181 CYS A 188 -1 O SER A 184 N VAL A 176
SHEET 1 D 7 ARG A 260 ILE A 264 0
SHEET 2 D 7 ALA A 252 CYS A 256 -1 N ALA A 252 O ILE A 264
SHEET 3 D 7 GLU A 160 LYS A 165 -1 N SER A 162 O PHE A 255
SHEET 4 D 7 GLY A 190 SER A 194 -1 O VAL A 193 N VAL A 161
SHEET 5 D 7 ILE A 218 ASN A 223 -1 O LEU A 219 N SER A 194
SHEET 6 D 7 MET A 233 THR A 235 -1 O MET A 233 N VAL A 220
SHEET 7 D 7 VAL B 210 LEU B 211 1 O VAL B 210 N VAL A 234
SHEET 1 E 7 VAL A 210 LEU A 211 0
SHEET 2 E 7 MET B 233 THR B 235 1 O VAL B 234 N VAL A 210
SHEET 3 E 7 ILE B 218 ASN B 223 -1 N VAL B 220 O MET B 233
SHEET 4 E 7 GLY B 190 SER B 194 -1 N GLY B 190 O ASN B 223
SHEET 5 E 7 VAL B 161 LYS B 165 -1 N VAL B 161 O VAL B 193
SHEET 6 E 7 ALA B 252 CYS B 256 -1 O LEU B 253 N GLU B 164
SHEET 7 E 7 ARG B 260 ILE B 264 -1 O ILE B 264 N ALA B 252
SHEET 1 F 4 ALA B 35 LEU B 39 0
SHEET 2 F 4 SER B 6 VAL B 11 1 N VAL B 7 O ALA B 35
SHEET 3 F 4 VAL B 79 GLY B 83 1 O LEU B 82 N VAL B 10
SHEET 4 F 4 VAL B 102 ASN B 106 1 O VAL B 105 N VAL B 81
SHEET 1 G 6 ARG B 150 ALA B 157 0
SHEET 2 G 6 ARG B 134 GLN B 147 -1 N LEU B 141 O ALA B 157
SHEET 3 G 6 ARG B 269 ARG B 283 -1 O GLU B 271 N VAL B 144
SHEET 4 G 6 ILE B 241 ILE B 245 -1 N ILE B 241 O VAL B 272
SHEET 5 G 6 LEU B 172 ILE B 178 -1 N GLU B 177 O ALA B 242
SHEET 6 G 6 ARG B 181 CYS B 188 -1 O PHE B 186 N VAL B 174
CRYST1 140.176 69.443 106.433 90.00 130.29 90.00 C 1 2 1 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 0.007134 0.000000 0.006048 0.00000
SCALE2 0.000000 0.014400 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012318 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
