HEADER LIGASE/LIGASE INHIBITOR 30-JUN-13 4LH7
TITLE CRYSTAL STRUCTURE OF A LIGA INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ADENYLATION DOMAIN, UNP RESIDUES 1-323;
COMPND 5 SYNONYM: POLYDEOXYRIBONUCLEOTIDE SYNTHASE [NAD(+)];
COMPND 6 EC: 6.5.1.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS;
SOURCE 3 ORGANISM_TAXID: 226185;
SOURCE 4 STRAIN: ATCC 700802 / V583;
SOURCE 5 GENE: EF_0722, LIGA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS PROTEIN-INHIBITOR COMPLEX, LIGASE-LIGASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.A.BORIACK-SJODIN,D.B.PRINCE
REVDAT 4 28-FEB-24 4LH7 1 REMARK
REVDAT 3 13-JAN-21 4LH7 1 SOURCE REMARK LINK
REVDAT 2 08-JAN-14 4LH7 1 JRNL
REVDAT 1 25-DEC-13 4LH7 0
JRNL AUTH K.MURPHY-BENENATO,H.WANG,H.M.MCGUIRE,H.E.DAVIS,N.GAO,
JRNL AUTH 2 D.B.PRINCE,H.JAHIC,S.S.STOKES,P.A.BORIACK-SJODIN
JRNL TITL IDENTIFICATION THROUGH STRUCTURE-BASED METHODS OF A
JRNL TITL 2 BACTERIAL NAD(+)-DEPENDENT DNA LIGASE INHIBITOR THAT AVOIDS
JRNL TITL 3 KNOWN RESISTANCE MUTATIONS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 24 360 2014
JRNL REFN ISSN 0960-894X
JRNL PMID 24287382
JRNL DOI 10.1016/J.BMCL.2013.11.007
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 25480
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 + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1369
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1661
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 84
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2579
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.21000
REMARK 3 B22 (A**2) : -0.05000
REMARK 3 B33 (A**2) : 0.27000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.196
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.169
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.368
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2720 ; 0.006 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1858 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3697 ; 0.992 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4517 ; 0.761 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 330 ; 5.296 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 140 ;33.498 ;24.357
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 464 ;12.963 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;12.305 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 396 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3071 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 553 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 322
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5950 38.9110 17.3160
REMARK 3 T TENSOR
REMARK 3 T11: 0.0477 T22: 0.0076
REMARK 3 T33: 0.0412 T12: -0.0073
REMARK 3 T13: -0.0084 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.3941 L22: 0.5585
REMARK 3 L33: 0.5674 L12: -0.3556
REMARK 3 L13: 0.1195 L23: -0.1077
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.0083 S13: -0.0835
REMARK 3 S21: -0.0343 S22: 0.0034 S23: 0.0793
REMARK 3 S31: 0.0225 S32: -0.0549 S33: -0.0033
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4LH7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080625.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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 : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26859
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 48.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.24900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-32% PEG4000, 0.2M AMMONIUM ACETATE,
REMARK 280 0.1M SODIUM ACETATE PH 5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K, PH 5.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 68.04250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.04250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 24.41900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.51250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.41900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.51250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.04250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.41900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 52.51250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.04250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.41900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 52.51250
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 571 LIES ON A SPECIAL POSITION.
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 323
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 NA A 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 218 O
REMARK 620 2 ARG A 220 O 97.7
REMARK 620 3 HOH A 535 O 159.6 82.5
REMARK 620 4 HOH A 562 O 98.2 80.1 61.6
REMARK 620 5 HOH A 596 O 88.1 165.6 87.5 86.0
REMARK 620 6 HOH A 627 O 102.7 92.1 97.7 158.6 99.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 276 O
REMARK 620 2 SER A 279 OG 105.2
REMARK 620 3 HOH A 543 O 71.5 81.2
REMARK 620 4 HOH A 587 O 96.5 157.7 101.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1X8 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NMN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LH6 RELATED DB: PDB
REMARK 900 INITIAL HIT FROM VIRTUAL SCREEN
DBREF 4LH7 A 1 323 UNP Q837V6 DNLJ_ENTFA 1 323
SEQRES 1 A 323 MET GLU GLN GLN PRO LEU THR LEU THR ALA ALA THR THR
SEQRES 2 A 323 ARG ALA GLN GLU LEU ARG LYS GLN LEU ASN GLN TYR SER
SEQRES 3 A 323 HIS GLU TYR TYR VAL LYS ASP GLN PRO SER VAL GLU ASP
SEQRES 4 A 323 TYR VAL TYR ASP ARG LEU TYR LYS GLU LEU VAL ASP ILE
SEQRES 5 A 323 GLU THR GLU PHE PRO ASP LEU ILE THR PRO ASP SER PRO
SEQRES 6 A 323 THR GLN ARG VAL GLY GLY LYS VAL LEU SER GLY PHE GLU
SEQRES 7 A 323 LYS ALA PRO HIS ASP ILE PRO MET TYR SER LEU ASN ASP
SEQRES 8 A 323 GLY PHE SER LYS GLU ASP ILE PHE ALA PHE ASP GLU ARG
SEQRES 9 A 323 VAL ARG LYS ALA ILE GLY LYS PRO VAL ALA TYR CYS CYS
SEQRES 10 A 323 GLU LEU LYS ILE ASP GLY LEU ALA ILE SER LEU ARG TYR
SEQRES 11 A 323 GLU ASN GLY VAL PHE VAL ARG GLY ALA THR ARG GLY ASP
SEQRES 12 A 323 GLY THR VAL GLY GLU ASN ILE THR GLU ASN LEU ARG THR
SEQRES 13 A 323 VAL ARG SER VAL PRO MET ARG LEU THR GLU PRO ILE SER
SEQRES 14 A 323 VAL GLU VAL ARG GLY GLU CYS TYR MET PRO LYS GLN SER
SEQRES 15 A 323 PHE VAL ALA LEU ASN GLU GLU ARG GLU GLU ASN GLY GLN
SEQRES 16 A 323 ASP ILE PHE ALA ASN PRO ARG ASN ALA ALA ALA GLY SER
SEQRES 17 A 323 LEU ARG GLN LEU ASP THR LYS ILE VAL ALA LYS ARG ASN
SEQRES 18 A 323 LEU ASN THR PHE LEU TYR THR VAL ALA ASP PHE GLY PRO
SEQRES 19 A 323 MET LYS ALA LYS THR GLN PHE GLU ALA LEU GLU GLU LEU
SEQRES 20 A 323 SER ALA ILE GLY PHE ARG THR ASN PRO GLU ARG GLN LEU
SEQRES 21 A 323 CYS GLN SER ILE ASP GLU VAL TRP ALA TYR ILE GLU GLU
SEQRES 22 A 323 TYR HIS GLU LYS ARG SER THR LEU PRO TYR GLU ILE ASP
SEQRES 23 A 323 GLY ILE VAL ILE LYS VAL ASN GLU PHE ALA LEU GLN ASP
SEQRES 24 A 323 GLU LEU GLY PHE THR VAL LYS ALA PRO ARG TRP ALA ILE
SEQRES 25 A 323 ALA TYR LYS PHE PRO PRO GLU GLU ALA GLU THR
HET 1X8 A 401 16
HET NMN A 402 22
HET NA A 403 1
HET NA A 404 1
HETNAM 1X8 4-AMINOTHIENO[3,2-C]PYRIDINE-2,7-DICARBOXAMIDE
HETNAM NMN BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE
HETNAM NA SODIUM ION
HETSYN NMN NICOTINAMIDE MONONUCLEOTIDE
FORMUL 2 1X8 C9 H8 N4 O2 S
FORMUL 3 NMN C11 H16 N2 O8 P 1+
FORMUL 4 NA 2(NA 1+)
FORMUL 6 HOH *159(H2 O)
HELIX 1 1 THR A 7 VAL A 31 1 25
HELIX 2 2 GLU A 38 PHE A 56 1 19
HELIX 3 3 PRO A 57 ILE A 60 5 4
HELIX 4 4 SER A 64 VAL A 69 5 6
HELIX 5 5 SER A 94 GLY A 110 1 17
HELIX 6 6 ILE A 150 THR A 156 1 7
HELIX 7 7 PRO A 179 GLY A 194 1 16
HELIX 8 8 ASN A 200 ARG A 210 1 11
HELIX 9 9 ASP A 213 ARG A 220 1 8
HELIX 10 10 THR A 239 GLY A 251 1 13
HELIX 11 11 SER A 263 ARG A 278 1 16
HELIX 12 12 SER A 279 LEU A 281 5 3
HELIX 13 13 GLU A 294 GLY A 302 1 9
HELIX 14 14 PRO A 318 GLU A 322 5 5
SHEET 1 A 2 LYS A 79 PRO A 81 0
SHEET 2 A 2 VAL A 146 GLU A 148 -1 O GLY A 147 N ALA A 80
SHEET 1 B 5 ASP A 91 GLY A 92 0
SHEET 2 B 5 ALA A 311 LYS A 315 1 O LYS A 315 N GLY A 92
SHEET 3 B 5 ILE A 285 VAL A 292 -1 N ILE A 288 O TYR A 314
SHEET 4 B 5 TYR A 115 ILE A 121 -1 N CYS A 116 O LYS A 291
SHEET 5 B 5 GLN A 259 CYS A 261 -1 O CYS A 261 N TYR A 115
SHEET 1 C 4 VAL A 134 THR A 140 0
SHEET 2 C 4 LEU A 124 GLU A 131 -1 N ARG A 129 O ARG A 137
SHEET 3 C 4 VAL A 170 TYR A 177 -1 O CYS A 176 N LEU A 124
SHEET 4 C 4 ASN A 223 VAL A 229 -1 O THR A 228 N ARG A 173
LINK O ALA A 218 NA NA A 403 1555 1555 2.45
LINK O ARG A 220 NA NA A 403 1555 1555 2.13
LINK O GLU A 276 NA NA A 404 1555 1555 2.37
LINK OG SER A 279 NA NA A 404 1555 1555 2.39
LINK NA NA A 403 O HOH A 535 1555 1555 2.54
LINK NA NA A 403 O HOH A 562 1555 1555 2.82
LINK NA NA A 403 O HOH A 596 1555 1555 2.19
LINK NA NA A 403 O HOH A 627 1555 1555 2.25
LINK NA NA A 404 O HOH A 543 1555 1555 2.44
LINK NA NA A 404 O HOH A 587 1555 1555 2.41
SITE 1 AC1 9 TYR A 87 LEU A 89 GLU A 118 LEU A 119
SITE 2 AC1 9 LYS A 120 ILE A 121 GLU A 175 TYR A 227
SITE 3 AC1 9 LYS A 291
SITE 1 AC2 13 TYR A 25 SER A 26 TYR A 29 TYR A 30
SITE 2 AC2 13 VAL A 37 ASP A 39 TYR A 42 ASP A 43
SITE 3 AC2 13 ARG A 158 HOH A 554 HOH A 561 HOH A 581
SITE 4 AC2 13 HOH A 634
SITE 1 AC3 6 ALA A 218 ARG A 220 HOH A 535 HOH A 562
SITE 2 AC3 6 HOH A 596 HOH A 627
SITE 1 AC4 4 GLU A 276 SER A 279 HOH A 543 HOH A 587
CRYST1 48.838 105.025 136.085 90.00 90.00 90.00 C 2 2 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 0.020476 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009522 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007348 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
