HEADER TRANSFERASE/TRANSFERASE INHIBITOR 15-DEC-13 4O18
TITLE STRUCTURAL BASIS FOR RESISTANCE TO DIVERSE CLASSES OF NAMPT INHIBITORS
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;
COMPND 8 MUTATION: 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-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.OH,M.COONS,B.BRILLANTES,W.WANG
REVDAT 2 28-FEB-24 4O18 1 REMARK SEQADV
REVDAT 1 22-OCT-14 4O18 0
JRNL AUTH W.WANG,K.ELKINS,A.OH,Y.C.HO,J.WU,H.LI,Y.XIAO,M.KWONG,
JRNL AUTH 2 M.COONS,B.BRILLANTES,E.CHENG,L.CROCKER,P.S.DRAGOVICH,
JRNL AUTH 3 D.SAMPATH,X.ZHENG,K.W.BAIR,T.O'BRIEN,L.D.BELMONT
JRNL TITL STRUCTURAL BASIS FOR RESISTANCE TO DIVERSE CLASSES OF NAMPT
JRNL TITL 2 INHIBITORS.
JRNL REF PLOS ONE V. 9 09366 2014
JRNL REFN ESSN 1932-6203
JRNL PMID 25285661
JRNL DOI 10.1371/JOURNAL.PONE.0109366
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 82.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 72644
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3906
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 82.4282 - 5.9661 0.90 4417 213 0.1765 0.1782
REMARK 3 2 5.9661 - 4.7356 0.88 4318 276 0.1488 0.1567
REMARK 3 3 4.7356 - 4.1370 0.86 4231 194 0.1391 0.1754
REMARK 3 4 4.1370 - 3.7588 0.87 4248 239 0.1473 0.1735
REMARK 3 5 3.7588 - 3.4894 0.89 4366 256 0.1507 0.2156
REMARK 3 6 3.4894 - 3.2836 0.89 4400 226 0.1631 0.1943
REMARK 3 7 3.2836 - 3.1192 0.92 4542 231 0.1744 0.2031
REMARK 3 8 3.1192 - 2.9834 0.92 4558 235 0.1658 0.2004
REMARK 3 9 2.9834 - 2.8685 0.93 4523 265 0.1834 0.2417
REMARK 3 10 2.8685 - 2.7695 0.94 4588 255 0.1849 0.2276
REMARK 3 11 2.7695 - 2.6829 0.94 4698 241 0.1713 0.2345
REMARK 3 12 2.6829 - 2.6062 0.95 4641 232 0.1626 0.2044
REMARK 3 13 2.6062 - 2.5376 0.95 4705 238 0.1748 0.2331
REMARK 3 14 2.5376 - 2.4757 0.96 4733 260 0.1768 0.2316
REMARK 3 15 2.4757 - 2.4194 0.96 4684 252 0.1809 0.2543
REMARK 3 16 2.4194 - 2.3679 0.96 4720 270 0.1849 0.2418
REMARK 3 17 2.3679 - 2.3206 0.96 4623 285 0.1822 0.2211
REMARK 3 18 2.3206 - 2.2768 0.95 4742 218 0.1836 0.2403
REMARK 3 19 2.2768 - 2.2361 0.96 4677 236 0.1876 0.2282
REMARK 3 20 2.2361 - 2.1982 0.95 4787 234 0.1886 0.2396
REMARK 3 21 2.1982 - 2.1627 0.96 4675 225 0.1951 0.2414
REMARK 3 22 2.1627 - 2.1295 0.96 4693 268 0.1993 0.2611
REMARK 3 23 2.1295 - 2.0981 0.95 4654 263 0.2176 0.2682
REMARK 3 24 2.0981 - 2.0686 0.95 4660 234 0.2190 0.2703
REMARK 3 25 2.0686 - 2.0406 0.95 4759 272 0.2255 0.2768
REMARK 3 26 2.0406 - 2.0141 0.95 4631 224 0.2307 0.2397
REMARK 3 27 2.0141 - 1.9889 0.95 4726 222 0.2330 0.2808
REMARK 3 28 1.9889 - 1.9650 0.95 4629 250 0.2431 0.3002
REMARK 3 29 1.9650 - 1.9421 0.95 4650 240 0.2531 0.2946
REMARK 3 30 1.9421 - 1.9200 0.95 4708 248 0.2691 0.3010
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.340
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 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 : 0.007 7724
REMARK 3 ANGLE : 1.036 10463
REMARK 3 CHIRALITY : 0.072 1148
REMARK 3 PLANARITY : 0.005 1327
REMARK 3 DIHEDRAL : 12.643 2845
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 8:487 OR RESID 701:1078 OR
REMARK 3 RESID 601:603 ) ) OR ( CHAIN B AND ( RESID 8:486 OR
REMARK 3 RESID 701:1059 OR RESID 601:603 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6263 1.2047 22.5315
REMARK 3 T TENSOR
REMARK 3 T11: 0.0102 T22: 0.0053
REMARK 3 T33: 0.0086 T12: -0.0050
REMARK 3 T13: -0.0026 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.0611 L22: 0.0537
REMARK 3 L33: 0.0832 L12: 0.0075
REMARK 3 L13: -0.0049 L23: 0.0185
REMARK 3 S TENSOR
REMARK 3 S11: 0.0262 S12: -0.0155 S13: -0.0031
REMARK 3 S21: -0.0241 S22: 0.0238 S23: -0.0294
REMARK 3 S31: -0.0016 S32: 0.0764 S33: 0.0653
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 4O18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JAN-13
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 : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.973973
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN COOLED DUAL
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77889
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.920
REMARK 200 RESOLUTION RANGE LOW (A) : 82.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : NULL
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) : 1.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
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 (%): 46.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM PHOSPHATE, PH 8.6, 25%
REMARK 280 POLYETHYLENE GLYCOL 3350, 0.2M NACL, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 292K
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 52.89100
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: 9950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33120 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 488
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 GLU B 487
REMARK 465 ALA B 488
REMARK 465 ALA B 489
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 GLU A 487 CG CD OE1 OE2
REMARK 470 VAL B 52 CB CG1 CG2
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 OD1 ASP A 354 O HOH A 842 2.07
REMARK 500 O HOH A 967 O HOH B 826 2.10
REMARK 500 O LEU B 486 O HOH B 898 2.11
REMARK 500 O HOH A 790 O HOH A 966 2.11
REMARK 500 O HOH B 910 O HOH B 992 2.13
REMARK 500 O HOH B 840 O HOH B 905 2.14
REMARK 500 O HOH A 735 O HOH B 826 2.15
REMARK 500 O HOH A 966 O HOH B 816 2.15
REMARK 500 O HOH A 789 O HOH A 892 2.16
REMARK 500 O HOH B 901 O HOH B 924 2.16
REMARK 500 O HOH B 738 O HOH B 1006 2.18
REMARK 500 O HOH A 1032 O HOH B 999 2.18
REMARK 500 O HOH B 808 O HOH B 952 2.19
REMARK 500 O HOH B 1013 O HOH B 1016 2.19
REMARK 500 O HOH A 842 O HOH A 971 2.19
REMARK 500 OD1 ASP B 354 O HOH B 799 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 TYR A 54 70.03 56.74
REMARK 500 VAL A 95 5.65 -50.31
REMARK 500 TYR A 231 -57.87 -128.11
REMARK 500 PHE A 269 62.32 -115.43
REMARK 500 GLU A 293 -64.23 -136.81
REMARK 500 ALA A 306 59.69 -144.96
REMARK 500 ASP A 313 14.30 -151.51
REMARK 500 ASP A 416 71.12 -157.10
REMARK 500 TYR B 231 -57.74 -134.47
REMARK 500 PHE B 269 58.62 -118.11
REMARK 500 GLU B 293 -64.33 -135.51
REMARK 500 ASP B 313 20.66 -155.21
REMARK 500 ASP B 416 70.24 -156.92
REMARK 500 ASP B 420 88.56 -150.37
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 PO4 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 EDO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4O13 RELATED DB: PDB
REMARK 900 RELATED ID: 4O14 RELATED DB: PDB
REMARK 900 RELATED ID: 4O15 RELATED DB: PDB
REMARK 900 RELATED ID: 4O16 RELATED DB: PDB
REMARK 900 RELATED ID: 4O17 RELATED DB: PDB
REMARK 900 RELATED ID: 4O19 RELATED DB: PDB
REMARK 900 RELATED ID: 4O1A RELATED DB: PDB
REMARK 900 RELATED ID: 4O1B RELATED DB: PDB
REMARK 900 RELATED ID: 4O1C RELATED DB: PDB
REMARK 900 RELATED ID: 4O1D RELATED DB: PDB
REMARK 900 RELATED ID: 4O28 RELATED DB: PDB
DBREF 4O18 A 1 491 UNP P43490 NAMPT_HUMAN 1 491
DBREF 4O18 B 1 491 UNP P43490 NAMPT_HUMAN 1 491
SEQADV 4O18 ALA A 217 UNP P43490 GLY 217 ENGINEERED MUTATION
SEQADV 4O18 LEU A 492 UNP P43490 EXPRESSION TAG
SEQADV 4O18 GLU A 493 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS A 494 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS A 495 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS A 496 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS A 497 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS A 498 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS A 499 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS A 500 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS A 501 UNP P43490 EXPRESSION TAG
SEQADV 4O18 ALA B 217 UNP P43490 GLY 217 ENGINEERED MUTATION
SEQADV 4O18 LEU B 492 UNP P43490 EXPRESSION TAG
SEQADV 4O18 GLU B 493 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS B 494 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS B 495 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS B 496 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS B 497 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS B 498 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS B 499 UNP P43490 EXPRESSION TAG
SEQADV 4O18 HIS B 500 UNP P43490 EXPRESSION TAG
SEQADV 4O18 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 ALA 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 ALA 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 PO4 A 601 5
HET PO4 A 602 5
HET EDO A 603 4
HET PO4 B 601 5
HET PO4 B 602 5
HET EDO B 603 4
HETNAM PO4 PHOSPHATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PO4 4(O4 P 3-)
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 9 HOH *737(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 TYR A 142 5 5
HELIX 7 7 TRP A 143 ILE A 148 1 6
HELIX 8 8 ILE A 148 GLN A 154 1 7
HELIX 9 9 SER A 155 GLY A 181 1 27
HELIX 10 10 GLY A 185 TYR A 188 5 4
HELIX 11 11 SER A 200 LEU A 212 1 13
HELIX 12 12 VAL A 221 TYR A 231 1 11
HELIX 13 13 GLU A 246 ALA A 252 1 7
HELIX 14 14 TRP A 253 ASP A 256 5 4
HELIX 15 15 HIS A 257 PHE A 269 1 13
HELIX 16 16 ASP A 282 LYS A 289 1 8
HELIX 17 17 LEU A 295 SER A 301 1 7
HELIX 18 18 ASN A 316 PHE A 332 1 17
HELIX 19 19 ASP A 357 LYS A 371 1 15
HELIX 20 20 SER A 374 GLU A 376 5 3
HELIX 21 21 GLY A 383 GLN A 388 1 6
HELIX 22 22 ASP A 420 ARG A 424 5 5
HELIX 23 23 GLY A 446 GLU A 451 5 6
HELIX 24 24 SER A 472 ALA A 480 1 9
HELIX 25 25 LEU A 482 GLU A 487 1 6
HELIX 26 26 ASN B 10 ALA B 14 5 5
HELIX 27 27 ASP B 16 GLN B 25 5 10
HELIX 28 28 GLY B 61 LEU B 70 1 10
HELIX 29 29 THR B 76 PHE B 91 1 16
HELIX 30 30 ASN B 97 ASP B 109 1 13
HELIX 31 31 ASP B 138 TYR B 142 5 5
HELIX 32 32 TRP B 143 ILE B 148 1 6
HELIX 33 33 ILE B 148 GLN B 154 1 7
HELIX 34 34 SER B 155 GLY B 181 1 27
HELIX 35 35 GLY B 185 TYR B 188 5 4
HELIX 36 36 SER B 200 LEU B 212 1 13
HELIX 37 37 VAL B 221 TYR B 231 1 11
HELIX 38 38 GLU B 246 ALA B 252 1 7
HELIX 39 39 TRP B 253 ASP B 256 5 4
HELIX 40 40 HIS B 257 PHE B 269 1 13
HELIX 41 41 ASP B 282 LYS B 289 1 8
HELIX 42 42 LEU B 295 VAL B 300 1 6
HELIX 43 43 ASN B 316 PHE B 332 1 17
HELIX 44 44 ASP B 357 LYS B 371 1 15
HELIX 45 45 SER B 374 GLU B 376 5 3
HELIX 46 46 GLY B 383 GLN B 388 1 6
HELIX 47 47 ASP B 420 ARG B 424 5 5
HELIX 48 48 GLY B 446 GLU B 451 5 6
HELIX 49 49 SER B 472 GLN B 481 1 10
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 36 O LYS A 400
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 VAL A 461 N ILE A 116
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 GLY A 381
SHEET 4 C 5 LEU A 308 ARG A 311 1 N ILE A 310 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 TYR B 36 O LYS B 400
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 PHE B 462 N ILE B 116
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 ILE B 310 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 7 GLU A 246 HIS A 247 ARG A 311 HOH A 783
SITE 2 AC1 7 HOH A 809 HOH A 849 TYR B 18
SITE 1 AC2 10 ARG A 40 ARG A 392 SER A 398 LYS A 400
SITE 2 AC2 10 HOH A 726 HOH A 775 HOH A 789 HOH A 816
SITE 3 AC2 10 HOH A 851 HOH A 994
SITE 1 AC3 5 PHE A 123 VAL A 124 ARG A 434 ASN A 479
SITE 2 AC3 5 HOH A 773
SITE 1 AC4 8 ARG A 196 HOH A 809 ARG B 392 SER B 398
SITE 2 AC4 8 LYS B 400 HOH B 740 HOH B 803 HOH B1048
SITE 1 AC5 10 TYR A 18 HOH A 726 HOH A 840 ARG B 196
SITE 2 AC5 10 GLU B 246 HIS B 247 ARG B 311 ASP B 313
SITE 3 AC5 10 HOH B 777 HOH B 929
SITE 1 AC6 1 ASN B 479
CRYST1 60.308 105.782 82.821 90.00 96.10 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 0.016582 0.000000 0.001771 0.00000
SCALE2 0.000000 0.009453 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012143 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
