HEADER TRANSFERASE/TRANSFERASE INHIBITOR 08-JUN-13 4L4L
TITLE STRUCTURAL ANALYSIS OF A PHOSPHORIBOSYLATED INHIBITOR IN COMPLEX WITH
TITLE 2 HUMAN NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NAMPRTASE, NAMPT, PRE-B-CELL COLONY-ENHANCING FACTOR 1, PRE-
COMPND 5 B CELL-ENHANCING FACTOR, VISFATIN;
COMPND 6 EC: 2.4.2.12;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NAMPT, PBEF, PBEF1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE, INHIBITOR PRPP ADDUCT, ACTIVE SITE, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.OH,Y.HO,M.ZAK,Y.LIU,P.YUEN,X.ZHENG,S.P.DRAGOVICH,W.WANG
REVDAT 3 28-FEB-24 4L4L 1 REMARK SEQADV
REVDAT 2 22-OCT-14 4L4L 1 JRNL
REVDAT 1 11-JUN-14 4L4L 0
JRNL AUTH A.OH,Y.C.HO,M.ZAK,Y.LIU,X.CHEN,P.W.YUEN,X.ZHENG,Y.LIU,
JRNL AUTH 2 P.S.DRAGOVICH,W.WANG
JRNL TITL STRUCTURAL AND BIOCHEMICAL ANALYSES OF THE CATALYSIS AND
JRNL TITL 2 POTENCY IMPACT OF INHIBITOR PHOSPHORIBOSYLATION BY HUMAN
JRNL TITL 3 NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE.
JRNL REF CHEMBIOCHEM V. 15 1121 2014
JRNL REFN ISSN 1439-4227
JRNL PMID 24797455
JRNL DOI 10.1002/CBIC.201402023
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 58463
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2926
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.8569 - 5.8490 0.99 2687 147 0.1784 0.1928
REMARK 3 2 5.8490 - 4.6448 1.00 2676 146 0.1593 0.2003
REMARK 3 3 4.6448 - 4.0583 1.00 2693 135 0.1536 0.1683
REMARK 3 4 4.0583 - 3.6876 1.00 2669 144 0.1677 0.1933
REMARK 3 5 3.6876 - 3.4234 1.00 2679 131 0.1719 0.2236
REMARK 3 6 3.4234 - 3.2217 1.00 2629 142 0.1813 0.1954
REMARK 3 7 3.2217 - 3.0604 1.00 2718 121 0.1813 0.2100
REMARK 3 8 3.0604 - 2.9272 1.00 2636 149 0.1911 0.2369
REMARK 3 9 2.9272 - 2.8145 1.00 2673 135 0.2026 0.2595
REMARK 3 10 2.8145 - 2.7174 0.99 2625 143 0.1962 0.2479
REMARK 3 11 2.7174 - 2.6325 0.99 2660 137 0.1983 0.2770
REMARK 3 12 2.6325 - 2.5573 0.99 2639 135 0.1957 0.2725
REMARK 3 13 2.5573 - 2.4900 0.99 2655 123 0.1890 0.2556
REMARK 3 14 2.4900 - 2.4292 0.99 2631 157 0.1964 0.2590
REMARK 3 15 2.4292 - 2.3740 0.99 2619 141 0.2070 0.2700
REMARK 3 16 2.3740 - 2.3235 0.99 2656 130 0.2138 0.2588
REMARK 3 17 2.3235 - 2.2770 0.99 2622 146 0.2242 0.2802
REMARK 3 18 2.2770 - 2.2340 0.99 2570 145 0.2277 0.2530
REMARK 3 19 2.2340 - 2.1941 0.99 2672 147 0.2425 0.2801
REMARK 3 20 2.1941 - 2.1570 0.98 2567 134 0.2646 0.3086
REMARK 3 21 2.1570 - 2.1222 0.96 2561 138 0.2845 0.3423
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 25.58
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.780
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) : 31.46920
REMARK 3 B22 (A**2) : 6.42760
REMARK 3 B33 (A**2) : -0.10630
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.21450
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 7843
REMARK 3 ANGLE : 0.833 10636
REMARK 3 CHIRALITY : 0.058 1158
REMARK 3 PLANARITY : 0.004 1348
REMARK 3 DIHEDRAL : 11.871 2871
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A OR CHAIN B OR CHAIN S OR CHAIN L
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3220 1.2252 22.5677
REMARK 3 T TENSOR
REMARK 3 T11: -0.0119 T22: -0.0001
REMARK 3 T33: -0.0271 T12: -0.0171
REMARK 3 T13: -0.0055 T23: 0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 0.0827 L22: 0.0795
REMARK 3 L33: 0.1213 L12: 0.0097
REMARK 3 L13: 0.0006 L23: 0.0363
REMARK 3 S TENSOR
REMARK 3 S11: 0.0547 S12: -0.0134 S13: -0.0031
REMARK 3 S21: -0.0500 S22: 0.0267 S23: -0.0704
REMARK 3 S31: -0.0090 S32: 0.0906 S33: 0.1187
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4L4L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080173.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12719
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58463
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
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) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2UL + 0.2UL DROPS CONTAINING 6MG/ML
REMARK 280 NAMPT, 0.1M SODIUM PHOSPHATE, 25-29% POLYETHYLENE GLYCOL 3350,
REMARK 280 0.2M NACL, 1MM LIGAND COMPOUND, PH 8.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 292K, VAPOR DIFFUSION, SITTING DROP
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 53.42850
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: 10030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33000 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 MET A 1
REMARK 465 ASN A 2
REMARK 465 PRO A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 GLU A 6
REMARK 465 ALA A 7
REMARK 465 THR A 44
REMARK 465 GLU A 45
REMARK 465 ASN A 46
REMARK 465 SER A 47
REMARK 465 LYS A 48
REMARK 465 LEU A 49
REMARK 465 ARG A 50
REMARK 465 LYS A 51
REMARK 465 VAL A 52
REMARK 465 ALA A 489
REMARK 465 HIS A 490
REMARK 465 HIS A 491
REMARK 465 LEU A 492
REMARK 465 GLU A 493
REMARK 465 HIS A 494
REMARK 465 HIS A 495
REMARK 465 HIS A 496
REMARK 465 HIS A 497
REMARK 465 HIS A 498
REMARK 465 HIS A 499
REMARK 465 HIS A 500
REMARK 465 HIS A 501
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 PRO B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 GLU B 6
REMARK 465 ALA B 7
REMARK 465 LYS B 43
REMARK 465 THR B 44
REMARK 465 GLU B 45
REMARK 465 ASN B 46
REMARK 465 SER B 47
REMARK 465 LYS B 48
REMARK 465 LEU B 49
REMARK 465 ARG B 50
REMARK 465 LYS B 51
REMARK 465 HIS B 490
REMARK 465 HIS B 491
REMARK 465 LEU B 492
REMARK 465 GLU B 493
REMARK 465 HIS B 494
REMARK 465 HIS B 495
REMARK 465 HIS B 496
REMARK 465 HIS B 497
REMARK 465 HIS B 498
REMARK 465 HIS B 499
REMARK 465 HIS B 500
REMARK 465 HIS B 501
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 LYS A 43 CG CD CE NZ
REMARK 470 VAL B 52 CB CG1 CG2
REMARK 470 GLU B 487 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU B 135 O HOH B 881 2.15
REMARK 500 O2 PO4 A 603 O HOH A 760 2.19
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 ASP A 94 30.91 -98.87
REMARK 500 TYR A 231 -57.81 -131.81
REMARK 500 PHE A 269 59.98 -118.84
REMARK 500 GLU A 293 -62.05 -139.49
REMARK 500 ASP A 313 15.66 -146.42
REMARK 500 ASP A 416 73.74 -159.09
REMARK 500 ASP A 420 86.21 -155.31
REMARK 500 ASN A 439 -158.71 -88.79
REMARK 500 TYR B 231 -54.78 -128.81
REMARK 500 GLU B 293 -67.37 -132.07
REMARK 500 ASP B 313 21.20 -145.31
REMARK 500 ASP B 416 72.95 -154.25
REMARK 500 ASP B 420 86.44 -154.49
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 1XC A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1XC B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4L4M RELATED DB: PDB
DBREF 4L4L A 1 491 UNP P43490 NAMPT_HUMAN 1 491
DBREF 4L4L B 1 491 UNP P43490 NAMPT_HUMAN 1 491
SEQADV 4L4L LEU A 492 UNP P43490 EXPRESSION TAG
SEQADV 4L4L GLU A 493 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS A 494 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS A 495 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS A 496 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS A 497 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS A 498 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS A 499 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS A 500 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS A 501 UNP P43490 EXPRESSION TAG
SEQADV 4L4L LEU B 492 UNP P43490 EXPRESSION TAG
SEQADV 4L4L GLU B 493 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS B 494 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS B 495 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS B 496 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS B 497 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS B 498 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS B 499 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS B 500 UNP P43490 EXPRESSION TAG
SEQADV 4L4L HIS B 501 UNP P43490 EXPRESSION TAG
SEQRES 1 A 501 MET ASN PRO ALA ALA GLU ALA GLU PHE ASN ILE LEU LEU
SEQRES 2 A 501 ALA THR ASP SER TYR LYS VAL THR HIS TYR LYS GLN TYR
SEQRES 3 A 501 PRO PRO ASN THR SER LYS VAL TYR SER TYR PHE GLU CYS
SEQRES 4 A 501 ARG GLU LYS LYS THR GLU ASN SER LYS LEU ARG LYS VAL
SEQRES 5 A 501 LYS TYR GLU GLU THR VAL PHE TYR GLY LEU GLN TYR ILE
SEQRES 6 A 501 LEU ASN LYS TYR LEU LYS GLY LYS VAL VAL THR LYS GLU
SEQRES 7 A 501 LYS ILE GLN GLU ALA LYS ASP VAL TYR LYS GLU HIS PHE
SEQRES 8 A 501 GLN ASP ASP VAL PHE ASN GLU LYS GLY TRP ASN TYR ILE
SEQRES 9 A 501 LEU GLU LYS TYR ASP GLY HIS LEU PRO ILE GLU ILE LYS
SEQRES 10 A 501 ALA VAL PRO GLU GLY PHE VAL ILE PRO ARG GLY ASN VAL
SEQRES 11 A 501 LEU PHE THR VAL GLU ASN THR ASP PRO GLU CYS TYR TRP
SEQRES 12 A 501 LEU THR ASN TRP ILE GLU THR ILE LEU VAL GLN SER TRP
SEQRES 13 A 501 TYR PRO ILE THR VAL ALA THR ASN SER ARG GLU GLN LYS
SEQRES 14 A 501 LYS ILE LEU ALA LYS TYR LEU LEU GLU THR SER GLY ASN
SEQRES 15 A 501 LEU ASP GLY LEU GLU TYR LYS LEU HIS ASP PHE GLY TYR
SEQRES 16 A 501 ARG GLY VAL SER SER GLN GLU THR ALA GLY ILE GLY ALA
SEQRES 17 A 501 SER ALA HIS LEU VAL ASN PHE LYS GLY THR ASP THR VAL
SEQRES 18 A 501 ALA GLY LEU ALA LEU ILE LYS LYS TYR TYR GLY THR LYS
SEQRES 19 A 501 ASP PRO VAL PRO GLY TYR SER VAL PRO ALA ALA GLU HIS
SEQRES 20 A 501 SER THR ILE THR ALA TRP GLY LYS ASP HIS GLU LYS ASP
SEQRES 21 A 501 ALA PHE GLU HIS ILE VAL THR GLN PHE SER SER VAL PRO
SEQRES 22 A 501 VAL SER VAL VAL SER ASP SER TYR ASP ILE TYR ASN ALA
SEQRES 23 A 501 CYS GLU LYS ILE TRP GLY GLU ASP LEU ARG HIS LEU ILE
SEQRES 24 A 501 VAL SER ARG SER THR GLN ALA PRO LEU ILE ILE ARG PRO
SEQRES 25 A 501 ASP SER GLY ASN PRO LEU ASP THR VAL LEU LYS VAL LEU
SEQRES 26 A 501 GLU ILE LEU GLY LYS LYS PHE PRO VAL THR GLU ASN SER
SEQRES 27 A 501 LYS GLY TYR LYS LEU LEU PRO PRO TYR LEU ARG VAL ILE
SEQRES 28 A 501 GLN GLY ASP GLY VAL ASP ILE ASN THR LEU GLN GLU ILE
SEQRES 29 A 501 VAL GLU GLY MET LYS GLN LYS MET TRP SER ILE GLU ASN
SEQRES 30 A 501 ILE ALA PHE GLY SER GLY GLY GLY LEU LEU GLN LYS LEU
SEQRES 31 A 501 THR ARG ASP LEU LEU ASN CYS SER PHE LYS CYS SER TYR
SEQRES 32 A 501 VAL VAL THR ASN GLY LEU GLY ILE ASN VAL PHE LYS ASP
SEQRES 33 A 501 PRO VAL ALA ASP PRO ASN LYS ARG SER LYS LYS GLY ARG
SEQRES 34 A 501 LEU SER LEU HIS ARG THR PRO ALA GLY ASN PHE VAL THR
SEQRES 35 A 501 LEU GLU GLU GLY LYS GLY ASP LEU GLU GLU TYR GLY GLN
SEQRES 36 A 501 ASP LEU LEU HIS THR VAL PHE LYS ASN GLY LYS VAL THR
SEQRES 37 A 501 LYS SER TYR SER PHE ASP GLU ILE ARG LYS ASN ALA GLN
SEQRES 38 A 501 LEU ASN ILE GLU LEU GLU ALA ALA HIS HIS LEU GLU HIS
SEQRES 39 A 501 HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 501 MET ASN PRO ALA ALA GLU ALA GLU PHE ASN ILE LEU LEU
SEQRES 2 B 501 ALA THR ASP SER TYR LYS VAL THR HIS TYR LYS GLN TYR
SEQRES 3 B 501 PRO PRO ASN THR SER LYS VAL TYR SER TYR PHE GLU CYS
SEQRES 4 B 501 ARG GLU LYS LYS THR GLU ASN SER LYS LEU ARG LYS VAL
SEQRES 5 B 501 LYS TYR GLU GLU THR VAL PHE TYR GLY LEU GLN TYR ILE
SEQRES 6 B 501 LEU ASN LYS TYR LEU LYS GLY LYS VAL VAL THR LYS GLU
SEQRES 7 B 501 LYS ILE GLN GLU ALA LYS ASP VAL TYR LYS GLU HIS PHE
SEQRES 8 B 501 GLN ASP ASP VAL PHE ASN GLU LYS GLY TRP ASN TYR ILE
SEQRES 9 B 501 LEU GLU LYS TYR ASP GLY HIS LEU PRO ILE GLU ILE LYS
SEQRES 10 B 501 ALA VAL PRO GLU GLY PHE VAL ILE PRO ARG GLY ASN VAL
SEQRES 11 B 501 LEU PHE THR VAL GLU ASN THR ASP PRO GLU CYS TYR TRP
SEQRES 12 B 501 LEU THR ASN TRP ILE GLU THR ILE LEU VAL GLN SER TRP
SEQRES 13 B 501 TYR PRO ILE THR VAL ALA THR ASN SER ARG GLU GLN LYS
SEQRES 14 B 501 LYS ILE LEU ALA LYS TYR LEU LEU GLU THR SER GLY ASN
SEQRES 15 B 501 LEU ASP GLY LEU GLU TYR LYS LEU HIS ASP PHE GLY TYR
SEQRES 16 B 501 ARG GLY VAL SER SER GLN GLU THR ALA GLY ILE GLY ALA
SEQRES 17 B 501 SER ALA HIS LEU VAL ASN PHE LYS GLY THR ASP THR VAL
SEQRES 18 B 501 ALA GLY LEU ALA LEU ILE LYS LYS TYR TYR GLY THR LYS
SEQRES 19 B 501 ASP PRO VAL PRO GLY TYR SER VAL PRO ALA ALA GLU HIS
SEQRES 20 B 501 SER THR ILE THR ALA TRP GLY LYS ASP HIS GLU LYS ASP
SEQRES 21 B 501 ALA PHE GLU HIS ILE VAL THR GLN PHE SER SER VAL PRO
SEQRES 22 B 501 VAL SER VAL VAL SER ASP SER TYR ASP ILE TYR ASN ALA
SEQRES 23 B 501 CYS GLU LYS ILE TRP GLY GLU ASP LEU ARG HIS LEU ILE
SEQRES 24 B 501 VAL SER ARG SER THR GLN ALA PRO LEU ILE ILE ARG PRO
SEQRES 25 B 501 ASP SER GLY ASN PRO LEU ASP THR VAL LEU LYS VAL LEU
SEQRES 26 B 501 GLU ILE LEU GLY LYS LYS PHE PRO VAL THR GLU ASN SER
SEQRES 27 B 501 LYS GLY TYR LYS LEU LEU PRO PRO TYR LEU ARG VAL ILE
SEQRES 28 B 501 GLN GLY ASP GLY VAL ASP ILE ASN THR LEU GLN GLU ILE
SEQRES 29 B 501 VAL GLU GLY MET LYS GLN LYS MET TRP SER ILE GLU ASN
SEQRES 30 B 501 ILE ALA PHE GLY SER GLY GLY GLY LEU LEU GLN LYS LEU
SEQRES 31 B 501 THR ARG ASP LEU LEU ASN CYS SER PHE LYS CYS SER TYR
SEQRES 32 B 501 VAL VAL THR ASN GLY LEU GLY ILE ASN VAL PHE LYS ASP
SEQRES 33 B 501 PRO VAL ALA ASP PRO ASN LYS ARG SER LYS LYS GLY ARG
SEQRES 34 B 501 LEU SER LEU HIS ARG THR PRO ALA GLY ASN PHE VAL THR
SEQRES 35 B 501 LEU GLU GLU GLY LYS GLY ASP LEU GLU GLU TYR GLY GLN
SEQRES 36 B 501 ASP LEU LEU HIS THR VAL PHE LYS ASN GLY LYS VAL THR
SEQRES 37 B 501 LYS SER TYR SER PHE ASP GLU ILE ARG LYS ASN ALA GLN
SEQRES 38 B 501 LEU ASN ILE GLU LEU GLU ALA ALA HIS HIS LEU GLU HIS
SEQRES 39 B 501 HIS HIS HIS HIS HIS HIS HIS
HET 1XC A 601 43
HET PO4 A 602 5
HET PO4 A 603 5
HET EDO A 604 4
HET EDO A 605 4
HET EDO A 606 4
HET 1XC B 601 43
HET PO4 B 602 5
HET PO4 B 603 5
HETNAM 1XC 6-({4-[(3,5-DIFLUOROPHENYL)SULFONYL]BENZYL}CARBAMOYL)-
HETNAM 2 1XC 1-(5-O-PHOSPHONO-BETA-D-RIBOFURANOSYL)IMIDAZO[1,2-
HETNAM 3 1XC A]PYRIDIN-1-IUM
HETNAM PO4 PHOSPHATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 1XC 2(C26 H25 F2 N3 O10 P S 1+)
FORMUL 4 PO4 4(O4 P 3-)
FORMUL 6 EDO 3(C2 H6 O2)
FORMUL 12 HOH *470(H2 O)
HELIX 1 1 ASN A 10 ALA A 14 5 5
HELIX 2 2 ASP A 16 GLN A 25 5 10
HELIX 3 3 GLY A 61 LEU A 70 1 10
HELIX 4 4 THR A 76 GLN A 92 1 17
HELIX 5 5 ASN A 97 ASP A 109 1 13
HELIX 6 6 ASP A 138 THR A 145 5 8
HELIX 7 7 ILE A 148 GLN A 154 1 7
HELIX 8 8 SER A 155 GLY A 181 1 27
HELIX 9 9 GLY A 185 TYR A 188 5 4
HELIX 10 10 SER A 200 LEU A 212 1 13
HELIX 11 11 VAL A 221 TYR A 231 1 11
HELIX 12 12 GLU A 246 ALA A 252 1 7
HELIX 13 13 TRP A 253 ASP A 256 5 4
HELIX 14 14 HIS A 257 PHE A 269 1 13
HELIX 15 15 ASP A 282 LYS A 289 1 8
HELIX 16 16 LEU A 295 VAL A 300 1 6
HELIX 17 17 ASN A 316 PHE A 332 1 17
HELIX 18 18 ASP A 357 LYS A 371 1 15
HELIX 19 19 SER A 374 GLU A 376 5 3
HELIX 20 20 GLY A 383 GLN A 388 1 6
HELIX 21 21 ASP A 420 ARG A 424 5 5
HELIX 22 22 GLY A 446 GLU A 451 5 6
HELIX 23 23 SER A 472 ALA A 480 1 9
HELIX 24 24 LEU A 482 GLU A 487 1 6
HELIX 25 25 ASN B 10 ALA B 14 5 5
HELIX 26 26 ASP B 16 GLN B 25 5 10
HELIX 27 27 GLY B 61 TYR B 69 1 9
HELIX 28 28 THR B 76 PHE B 91 1 16
HELIX 29 29 ASN B 97 ASP B 109 1 13
HELIX 30 30 ASP B 138 TYR B 142 5 5
HELIX 31 31 TRP B 143 ILE B 148 1 6
HELIX 32 32 ILE B 148 GLN B 154 1 7
HELIX 33 33 SER B 155 GLY B 181 1 27
HELIX 34 34 GLY B 185 TYR B 188 5 4
HELIX 35 35 SER B 200 LEU B 212 1 13
HELIX 36 36 VAL B 221 TYR B 231 1 11
HELIX 37 37 GLU B 246 ALA B 252 1 7
HELIX 38 38 TRP B 253 ASP B 256 5 4
HELIX 39 39 HIS B 257 PHE B 269 1 13
HELIX 40 40 ASP B 282 LYS B 289 1 8
HELIX 41 41 LEU B 295 ILE B 299 5 5
HELIX 42 42 ASN B 316 PHE B 332 1 17
HELIX 43 43 ASP B 357 LYS B 371 1 15
HELIX 44 44 SER B 374 GLU B 376 5 3
HELIX 45 45 GLY B 383 GLN B 388 1 6
HELIX 46 46 ASP B 420 ARG B 424 5 5
HELIX 47 47 GLY B 446 GLU B 451 5 6
HELIX 48 48 SER B 472 ALA B 480 1 9
HELIX 49 49 LEU B 482 GLU B 487 1 6
SHEET 1 A 7 LEU A 409 ASN A 412 0
SHEET 2 A 7 CYS A 397 THR A 406 -1 N VAL A 404 O ILE A 411
SHEET 3 A 7 THR A 30 CYS A 39 -1 N TYR A 34 O TYR A 403
SHEET 4 A 7 VAL A 130 ASN A 136 -1 O VAL A 134 N SER A 35
SHEET 5 A 7 ILE A 114 ALA A 118 -1 N GLU A 115 O GLU A 135
SHEET 6 A 7 HIS A 459 LYS A 463 -1 O HIS A 459 N ALA A 118
SHEET 7 A 7 LYS A 466 VAL A 467 -1 O LYS A 466 N LYS A 463
SHEET 1 B 2 GLU A 56 VAL A 58 0
SHEET 2 B 2 VAL A 124 PRO A 126 -1 O ILE A 125 N THR A 57
SHEET 1 C 5 LEU A 190 ASP A 192 0
SHEET 2 C 5 ILE A 378 SER A 382 1 O PHE A 380 N HIS A 191
SHEET 3 C 5 LEU A 348 GLN A 352 1 N GLN A 352 O ALA A 379
SHEET 4 C 5 LEU A 308 ARG A 311 1 N LEU A 308 O ARG A 349
SHEET 5 C 5 VAL A 274 VAL A 277 1 N VAL A 274 O ILE A 309
SHEET 1 D 2 THR A 335 GLU A 336 0
SHEET 2 D 2 LYS A 342 LEU A 343 -1 O LEU A 343 N THR A 335
SHEET 1 E 2 SER A 431 ARG A 434 0
SHEET 2 E 2 PHE A 440 LEU A 443 -1 O VAL A 441 N HIS A 433
SHEET 1 F 7 LEU B 409 ASN B 412 0
SHEET 2 F 7 CYS B 397 THR B 406 -1 N VAL B 404 O ILE B 411
SHEET 3 F 7 THR B 30 CYS B 39 -1 N SER B 31 O VAL B 405
SHEET 4 F 7 VAL B 130 ASN B 136 -1 O VAL B 134 N SER B 35
SHEET 5 F 7 ILE B 114 ALA B 118 -1 N GLU B 115 O GLU B 135
SHEET 6 F 7 HIS B 459 LYS B 463 -1 O HIS B 459 N ALA B 118
SHEET 7 F 7 LYS B 466 VAL B 467 -1 O LYS B 466 N LYS B 463
SHEET 1 G 2 GLU B 56 VAL B 58 0
SHEET 2 G 2 VAL B 124 PRO B 126 -1 O ILE B 125 N THR B 57
SHEET 1 H 5 LEU B 190 ASP B 192 0
SHEET 2 H 5 ILE B 378 SER B 382 1 O PHE B 380 N HIS B 191
SHEET 3 H 5 LEU B 348 GLN B 352 1 N GLN B 352 O GLY B 381
SHEET 4 H 5 LEU B 308 ARG B 311 1 N LEU B 308 O ARG B 349
SHEET 5 H 5 VAL B 274 VAL B 277 1 N VAL B 274 O ILE B 309
SHEET 1 I 2 THR B 335 GLU B 336 0
SHEET 2 I 2 LYS B 342 LEU B 343 -1 O LEU B 343 N THR B 335
SHEET 1 J 2 SER B 431 ARG B 434 0
SHEET 2 J 2 PHE B 440 LEU B 443 -1 O LEU B 443 N SER B 431
SITE 1 AC1 29 TYR A 188 HIS A 191 PHE A 193 ARG A 196
SITE 2 AC1 29 ASP A 219 SER A 241 VAL A 242 ALA A 244
SITE 3 AC1 29 PRO A 273 SER A 275 ILE A 309 ARG A 311
SITE 4 AC1 29 ASP A 313 ILE A 351 GLY A 353 GLY A 383
SITE 5 AC1 29 GLY A 384 PO4 A 602 EDO A 605 HOH A 720
SITE 6 AC1 29 HOH A 739 HOH A 743 HOH A 757 HOH A 829
SITE 7 AC1 29 HOH A 934 TYR B 18 ARG B 392 PO4 B 603
SITE 8 AC1 29 HOH B 878
SITE 1 AC2 8 ARG A 196 GLU A 246 HIS A 247 ARG A 311
SITE 2 AC2 8 ASP A 313 1XC A 601 HOH A 749 TYR B 18
SITE 1 AC3 10 ARG A 40 ARG A 392 SER A 398 LYS A 400
SITE 2 AC3 10 HOH A 760 HOH A 762 HOH A 796 HOH A 865
SITE 3 AC3 10 HOH A 875 1XC B 601
SITE 1 AC4 5 PHE A 123 VAL A 124 ARG A 434 ASN A 479
SITE 2 AC4 5 HOH A 810
SITE 1 AC5 5 LYS A 189 ILE A 378 ALA A 379 1XC A 601
SITE 2 AC5 5 HOH A 893
SITE 1 AC6 3 PRO A 27 THR A 30 TYR A 142
SITE 1 AC7 26 TYR A 18 ARG A 392 PO4 A 603 HOH A 762
SITE 2 AC7 26 TYR B 188 HIS B 191 PHE B 193 ARG B 196
SITE 3 AC7 26 ASP B 219 SER B 241 VAL B 242 ALA B 244
SITE 4 AC7 26 SER B 275 ARG B 311 ASP B 313 GLY B 353
SITE 5 AC7 26 GLY B 383 GLY B 384 PO4 B 602 HOH B 715
SITE 6 AC7 26 HOH B 724 HOH B 727 HOH B 746 HOH B 766
SITE 7 AC7 26 HOH B 768 HOH B 791
SITE 1 AC8 6 TYR A 18 GLU B 246 HIS B 247 ARG B 311
SITE 2 AC8 6 1XC B 601 HOH B 717
SITE 1 AC9 9 1XC A 601 ARG B 40 ARG B 392 SER B 398
SITE 2 AC9 9 LYS B 400 HOH B 795 HOH B 842 HOH B 878
SITE 3 AC9 9 HOH B 926
CRYST1 60.215 106.857 83.021 90.00 96.53 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 0.016607 0.000000 0.001900 0.00000
SCALE2 0.000000 0.009358 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012124 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
