HEADER TRANSFERASE/TRANSFERASE INHIBITOR 26-JUL-13 4LVA
TITLE FRAGMENT-BASED IDENTIFICATION OF AMIDES DERIVED FROM TRANS-2-(PYRIDIN-
TITLE 2 3-YL)CYCLOPROPANECARBOXYLIC ACID AS POTENT INHIBITORS OF HUMAN
TITLE 3 NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE (NAMPT)
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, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.GIANNETTI,X.ZHENG,N.SKELTON,W.WANG,B.BRAVO,Y.FENG,J.GUNZNER-
AUTHOR 2 TOSTE,Y.HO,R.HUA,C.WANG,Q.ZHAO,B.M.LIEDERER,Y.LIU,T.O'BRIEN,J.OEH,
AUTHOR 3 D.SAMPATH,Y.SHEN,L.WANG,H.WU,Y.XIAO,P.YUEN,M.ZAK,G.ZHAO,
AUTHOR 4 P.S.DRAGOVICH
REVDAT 4 28-FEB-24 4LVA 1 REMARK SEQADV
REVDAT 3 24-JAN-18 4LVA 1 AUTHOR
REVDAT 2 02-OCT-13 4LVA 1 JRNL
REVDAT 1 25-SEP-13 4LVA 0
JRNL AUTH X.ZHENG,K.W.BAIR,P.BAUER,T.BAUMEISTER,K.K.BOWMAN,
JRNL AUTH 2 A.J.BUCKMELTER,M.CALIGIURI,K.H.CLODFELTER,Y.FENG,B.HAN,
JRNL AUTH 3 Y.C.HO,N.KLEY,H.LI,X.LIANG,B.M.LIEDERER,J.LIN,J.LY,
JRNL AUTH 4 T.O'BRIEN,J.OEH,A.OH,D.J.REYNOLDS,D.SAMPATH,G.SHARMA,
JRNL AUTH 5 N.SKELTON,C.C.SMITH,J.TREMAYNE,L.WANG,W.WANG,Z.WANG,H.WU,
JRNL AUTH 6 J.WU,Y.XIAO,G.YANG,P.W.YUEN,M.ZAK,P.S.DRAGOVICH
JRNL TITL IDENTIFICATION OF AMIDES DERIVED FROM
JRNL TITL 2 1H-PYRAZOLO[3,4-B]PYRIDINE-5-CARBOXYLIC ACID AS POTENT
JRNL TITL 3 INHIBITORS OF HUMAN NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE
JRNL TITL 4 (NAMPT).
JRNL REF BIOORG.MED.CHEM.LETT. V. 23 5488 2013
JRNL REFN ISSN 0960-894X
JRNL PMID 24021463
JRNL DOI 10.1016/J.BMCL.2013.08.074
REMARK 2
REMARK 2 RESOLUTION. 1.55 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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 151425
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 7612
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 46.3909 - 4.8141 1.00 4888 255 0.1878 0.1842
REMARK 3 2 4.8141 - 3.8217 1.00 4855 240 0.1585 0.1776
REMARK 3 3 3.8217 - 3.3387 1.00 4816 264 0.1695 0.1800
REMARK 3 4 3.3387 - 3.0335 1.00 4833 222 0.1743 0.2177
REMARK 3 5 3.0335 - 2.8161 1.00 4808 282 0.1796 0.2054
REMARK 3 6 2.8161 - 2.6501 1.00 4818 236 0.1758 0.2047
REMARK 3 7 2.6501 - 2.5174 1.00 4769 279 0.1704 0.2106
REMARK 3 8 2.5174 - 2.4078 1.00 4780 256 0.1666 0.2167
REMARK 3 9 2.4078 - 2.3152 1.00 4805 251 0.1710 0.1939
REMARK 3 10 2.3152 - 2.2353 1.00 4779 274 0.1644 0.2005
REMARK 3 11 2.2353 - 2.1654 1.00 4802 267 0.1617 0.1845
REMARK 3 12 2.1654 - 2.1035 1.00 4765 279 0.1703 0.2106
REMARK 3 13 2.1035 - 2.0481 1.00 4830 235 0.1690 0.1989
REMARK 3 14 2.0481 - 1.9981 1.00 4807 261 0.1660 0.1968
REMARK 3 15 1.9981 - 1.9527 1.00 4767 216 0.1679 0.2063
REMARK 3 16 1.9527 - 1.9111 1.00 4835 239 0.1715 0.2122
REMARK 3 17 1.9111 - 1.8729 1.00 4779 259 0.1775 0.2354
REMARK 3 18 1.8729 - 1.8376 1.00 4768 267 0.1785 0.2232
REMARK 3 19 1.8376 - 1.8048 1.00 4769 242 0.1760 0.2323
REMARK 3 20 1.8048 - 1.7742 1.00 4785 250 0.1812 0.2252
REMARK 3 21 1.7742 - 1.7455 1.00 4854 243 0.1817 0.2192
REMARK 3 22 1.7455 - 1.7187 1.00 4741 261 0.1901 0.2224
REMARK 3 23 1.7187 - 1.6934 1.00 4793 248 0.1943 0.2436
REMARK 3 24 1.6934 - 1.6696 1.00 4781 265 0.2016 0.2421
REMARK 3 25 1.6696 - 1.6470 1.00 4788 242 0.2049 0.2530
REMARK 3 26 1.6470 - 1.6256 1.00 4812 261 0.2102 0.2537
REMARK 3 27 1.6256 - 1.6053 1.00 4765 250 0.2202 0.2670
REMARK 3 28 1.6053 - 1.5859 1.00 4771 254 0.2248 0.2696
REMARK 3 29 1.5859 - 1.5675 1.00 4774 235 0.2357 0.2963
REMARK 3 30 1.5675 - 1.5500 0.99 4676 279 0.2446 0.2706
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.900
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 : 0.015 7831
REMARK 3 ANGLE : 1.596 10596
REMARK 3 CHIRALITY : 0.106 1147
REMARK 3 PLANARITY : 0.009 1334
REMARK 3 DIHEDRAL : 13.739 2868
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 8:486 OR RESID 603:610 ) ) OR
REMARK 3 ( CHAIN B AND ( RESID 8:487 OR RESID 603:610 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3574 -0.2921 22.6147
REMARK 3 T TENSOR
REMARK 3 T11: 0.0237 T22: 0.0460
REMARK 3 T33: 0.0446 T12: -0.0025
REMARK 3 T13: -0.0032 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.1630 L22: 0.3165
REMARK 3 L33: 0.2554 L12: 0.0606
REMARK 3 L13: -0.0559 L23: -0.0639
REMARK 3 S TENSOR
REMARK 3 S11: 0.0307 S12: -0.0244 S13: 0.0000
REMARK 3 S21: -0.0165 S22: -0.0093 S23: -0.0236
REMARK 3 S31: 0.0023 S32: 0.0575 S33: 0.0006
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 4LVA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081130.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-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 : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 (ACCEL DCM) WITH AN INDIRECTLY
REMARK 200 CRYO-COOLED FIRST CRYSTAL AND
REMARK 200 SAGITTALLY FOCUSING SECOND
REMARK 200 CRYSTAL
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 : 151480
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : 100.0
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) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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 (%): 47.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
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 COMPOUND, PH 8.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 53.39950
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: 12670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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 LYS A 43
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 GLU A 487
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 VAL B 52
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 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 O2 PO4 A 604 O2 EDO A 610 1.89
REMARK 500 O4 PO4 B 604 O2 EDO B 608 1.96
REMARK 500 O HOH B 930 O HOH B 1012 2.01
REMARK 500 O HOH A 919 O HOH A 1154 2.04
REMARK 500 O HOH B 895 O HOH B 932 2.04
REMARK 500 O HOH B 874 O HOH B 1065 2.05
REMARK 500 O HOH A 919 O HOH A 1014 2.06
REMARK 500 O HOH B 1060 O HOH B 1127 2.06
REMARK 500 O HOH A 960 O HOH A 988 2.06
REMARK 500 O HOH B 755 O HOH B 978 2.07
REMARK 500 O HOH A 1053 O HOH A 1076 2.08
REMARK 500 O HOH B 1071 O HOH B 1102 2.08
REMARK 500 O HOH B 938 O HOH B 1008 2.08
REMARK 500 O HOH A 944 O HOH A 1064 2.08
REMARK 500 O HOH B 967 O HOH B 1208 2.08
REMARK 500 O HOH B 1010 O HOH B 1196 2.10
REMARK 500 O HOH B 974 O HOH B 1023 2.10
REMARK 500 O HOH A 1005 O HOH A 1083 2.10
REMARK 500 OE1 GLU B 187 O HOH B 916 2.10
REMARK 500 NZ LYS A 42 O HOH A 1190 2.11
REMARK 500 O HOH A 934 O HOH A 998 2.11
REMARK 500 O HOH A 913 O HOH B 1123 2.11
REMARK 500 OE1 GLU B 8 O HOH B 981 2.12
REMARK 500 O HOH A 990 O HOH A 1015 2.12
REMARK 500 O HOH A 1093 O HOH B 951 2.13
REMARK 500 O LYS A 255 O HOH A 1054 2.13
REMARK 500 O HOH A 1108 O HOH A 1143 2.13
REMARK 500 O HOH B 841 O HOH B 1138 2.13
REMARK 500 O HOH A 1106 O HOH A 1129 2.14
REMARK 500 O HOH B 1044 O HOH B 1112 2.14
REMARK 500 O HOH A 940 O HOH A 1125 2.14
REMARK 500 O HOH A 1140 O HOH A 1146 2.14
REMARK 500 O HOH B 1029 O HOH B 1039 2.15
REMARK 500 OE2 GLU A 485 O HOH A 950 2.15
REMARK 500 O HOH A 736 O HOH A 1093 2.16
REMARK 500 O HOH B 1049 O HOH B 1124 2.16
REMARK 500 O HOH A 1047 O HOH A 1165 2.16
REMARK 500 O HOH B 960 O HOH B 995 2.17
REMARK 500 O HOH A 1157 O HOH A 1164 2.17
REMARK 500 O HOH B 990 O HOH B 1159 2.17
REMARK 500 O HOH A 856 O HOH A 875 2.17
REMARK 500 O2 EDO B 607 O HOH B 1038 2.17
REMARK 500 O HOH A 1085 O HOH B 935 2.18
REMARK 500 O HOH A 1004 O HOH B 1096 2.18
REMARK 500 OE1 GLU A 89 O HOH A 981 2.18
REMARK 500 O HOH B 1080 O HOH B 1100 2.18
REMARK 500 O HOH B 1120 O HOH B 1130 2.18
REMARK 500 O HOH B 960 O HOH B 1040 2.18
REMARK 500 O HOH B 977 O HOH B 1013 2.19
REMARK 500 O HOH A 791 O HOH A 1117 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1197 O HOH B 1063 2646 1.95
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 ALA A 14 40.69 -108.56
REMARK 500 TYR A 231 -61.15 -125.74
REMARK 500 GLU A 293 -71.25 -134.81
REMARK 500 ASP A 313 18.65 -152.96
REMARK 500 ASP A 416 74.18 -156.06
REMARK 500 ASP A 420 83.78 -154.27
REMARK 500 TYR B 231 -55.25 -125.96
REMARK 500 GLU B 293 -68.95 -134.35
REMARK 500 ASP B 313 19.88 -149.07
REMARK 500 ASP B 416 76.89 -161.31
REMARK 500 ASP B 420 88.71 -150.06
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 20M 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 PO4 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 EDO A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 20M B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 610
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LV9 RELATED DB: PDB
REMARK 900 RELATED ID: 4LVB RELATED DB: PDB
REMARK 900 RELATED ID: 4LVD RELATED DB: PDB
REMARK 900 RELATED ID: 4LVF RELATED DB: PDB
REMARK 900 RELATED ID: 4LVG RELATED DB: PDB
REMARK 900 RELATED ID: 4M6P RELATED DB: PDB
REMARK 900 RELATED ID: 4M6Q RELATED DB: PDB
DBREF 4LVA A 1 491 UNP P43490 NAMPT_HUMAN 1 491
DBREF 4LVA B 1 491 UNP P43490 NAMPT_HUMAN 1 491
SEQADV 4LVA LEU A 492 UNP P43490 EXPRESSION TAG
SEQADV 4LVA GLU A 493 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS A 494 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS A 495 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS A 496 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS A 497 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS A 498 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS A 499 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS A 500 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS A 501 UNP P43490 EXPRESSION TAG
SEQADV 4LVA LEU B 492 UNP P43490 EXPRESSION TAG
SEQADV 4LVA GLU B 493 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS B 494 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS B 495 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS B 496 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS B 497 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS B 498 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS B 499 UNP P43490 EXPRESSION TAG
SEQADV 4LVA HIS B 500 UNP P43490 EXPRESSION TAG
SEQADV 4LVA 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 20M A 601 34
HET PO4 A 602 5
HET PO4 A 603 5
HET PO4 A 604 5
HET EDO A 605 4
HET EDO A 606 4
HET EDO A 607 4
HET EDO A 608 4
HET EDO A 609 4
HET EDO A 610 4
HET 20M B 601 34
HET PO4 B 602 5
HET PO4 B 603 5
HET PO4 B 604 5
HET EDO B 605 4
HET EDO B 606 4
HET EDO B 607 4
HET EDO B 608 4
HET EDO B 609 4
HET EDO B 610 4
HETNAM 20M N-(4-{[4-(PYRROLIDIN-1-YL)PIPERIDIN-1-
HETNAM 2 20M YL]SULFONYL}BENZYL)-2H-PYRIDO[4,3-E][1,2,4]THIADIAZIN-
HETNAM 3 20M 3-AMINE 1,1-DIOXIDE
HETNAM PO4 PHOSPHATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 20M 2(C22 H28 N6 O4 S2)
FORMUL 4 PO4 6(O4 P 3-)
FORMUL 7 EDO 12(C2 H6 O2)
FORMUL 23 HOH *1006(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 GLY A 194 VAL A 198 5 5
HELIX 12 12 SER A 200 VAL A 213 1 14
HELIX 13 13 VAL A 221 TYR A 231 1 11
HELIX 14 14 GLU A 246 ALA A 252 1 7
HELIX 15 15 TRP A 253 ASP A 256 5 4
HELIX 16 16 HIS A 257 PHE A 269 1 13
HELIX 17 17 ASP A 282 LYS A 289 1 8
HELIX 18 18 LEU A 295 VAL A 300 1 6
HELIX 19 19 ASN A 316 PHE A 332 1 17
HELIX 20 20 ASP A 357 LYS A 371 1 15
HELIX 21 21 SER A 374 GLU A 376 5 3
HELIX 22 22 GLY A 383 GLN A 388 1 6
HELIX 23 23 ASP A 420 ARG A 424 5 5
HELIX 24 24 GLY A 446 GLU A 451 5 6
HELIX 25 25 SER A 472 ALA A 480 1 9
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 GLN B 92 1 17
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 GLY B 194 VAL B 198 5 5
HELIX 37 37 SER B 200 LEU B 212 1 13
HELIX 38 38 VAL B 221 TYR B 231 1 11
HELIX 39 39 GLU B 246 ALA B 252 1 7
HELIX 40 40 TRP B 253 ASP B 256 5 4
HELIX 41 41 HIS B 257 PHE B 269 1 13
HELIX 42 42 ASP B 282 LYS B 289 1 8
HELIX 43 43 LEU B 295 VAL B 300 1 6
HELIX 44 44 ASN B 316 PHE B 332 1 17
HELIX 45 45 ASP B 357 LYS B 371 1 15
HELIX 46 46 SER B 374 GLU B 376 5 3
HELIX 47 47 GLY B 383 GLN B 388 1 6
HELIX 48 48 ASP B 420 ARG B 424 5 5
HELIX 49 49 GLY B 446 GLU B 451 5 6
HELIX 50 50 SER B 472 ALA B 480 1 9
HELIX 51 51 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 PHE A 132 N PHE A 37
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 PHE A 462 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 34 O SER B 402
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 VAL B 461 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 ALA B 379
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 VAL B 441 N HIS B 433
SITE 1 AC1 17 TYR A 188 HIS A 191 PHE A 193 ASP A 219
SITE 2 AC1 17 SER A 241 VAL A 242 ALA A 244 ALA A 245
SITE 3 AC1 17 SER A 275 ILE A 309 ARG A 311 ILE A 351
SITE 4 AC1 17 ALA A 379 EDO A 607 HOH A 712 HOH A 854
SITE 5 AC1 17 TYR B 18
SITE 1 AC2 10 ARG A 196 GLU A 246 HIS A 247 ARG A 311
SITE 2 AC2 10 HOH A 746 HOH A 761 HOH A 762 TYR B 18
SITE 3 AC2 10 HOH B 757 HOH B 776
SITE 1 AC3 12 ARG A 392 SER A 398 LYS A 400 EDO A 606
SITE 2 AC3 12 HOH A 719 HOH A 731 HOH A 736 HOH A 747
SITE 3 AC3 12 HOH A 753 HOH A1093 ARG B 196 PO4 B 603
SITE 1 AC4 12 PHE A 193 GLY A 194 ARG A 196 GLY A 197
SITE 2 AC4 12 GLY A 383 GLY A 384 EDO A 610 HOH A 850
SITE 3 AC4 12 HOH A 882 HOH A1072 HOH A1187 ARG B 392
SITE 1 AC5 5 GLU A 187 VAL A 213 ASN A 214 ARG A 477
SITE 2 AC5 5 HOH A1014
SITE 1 AC6 8 ARG A 40 ARG A 392 ASP A 393 ASN A 396
SITE 2 AC6 8 CYS A 397 PO4 A 603 HOH A 949 HOH A1093
SITE 1 AC7 8 LYS A 189 ILE A 309 ARG A 349 VAL A 350
SITE 2 AC7 8 ILE A 378 ALA A 379 20M A 601 HOH A 887
SITE 1 AC8 7 GLY A 315 PRO A 317 ASP A 354 GLY A 355
SITE 2 AC8 7 HOH A 836 HOH A 864 HOH B1038
SITE 1 AC9 6 PHE A 123 VAL A 124 ARG A 434 PHE A 440
SITE 2 AC9 6 ASN A 479 HOH A 837
SITE 1 BC1 10 ASP A 354 GLY A 355 GLY A 384 PO4 A 604
SITE 2 BC1 10 HOH A 734 HOH A 745 HOH A 850 HOH A 882
SITE 3 BC1 10 HOH B 964 HOH B1204
SITE 1 BC2 17 TYR A 18 TYR B 188 HIS B 191 PHE B 193
SITE 2 BC2 17 ARG B 196 ASP B 219 SER B 241 VAL B 242
SITE 3 BC2 17 ALA B 244 ALA B 245 ILE B 309 ARG B 311
SITE 4 BC2 17 ILE B 351 ALA B 379 HOH B 711 HOH B 787
SITE 5 BC2 17 HOH B1011
SITE 1 BC3 10 ARG A 196 HOH A 746 ARG B 392 SER B 398
SITE 2 BC3 10 LYS B 400 EDO B 605 HOH B 720 HOH B 739
SITE 3 BC3 10 HOH B 747 HOH B 776
SITE 1 BC4 11 TYR A 18 PO4 A 603 HOH A 719 HOH A 731
SITE 2 BC4 11 HOH A 759 ARG B 196 GLU B 246 HIS B 247
SITE 3 BC4 11 ARG B 311 HOH B 771 HOH B 775
SITE 1 BC5 13 ARG A 392 PHE B 193 GLY B 194 ARG B 196
SITE 2 BC5 13 GLY B 197 GLY B 383 GLY B 384 EDO B 608
SITE 3 BC5 13 HOH B 805 HOH B 843 HOH B 920 HOH B1000
SITE 4 BC5 13 HOH B1205
SITE 1 BC6 8 ARG B 40 ARG B 392 ASP B 393 ASN B 396
SITE 2 BC6 8 CYS B 397 SER B 398 PO4 B 602 EDO B 607
SITE 1 BC7 9 HIS A 247 SER A 248 THR A 251 HOH A 762
SITE 2 BC7 9 LYS B 400 CYS B 401 PHE B 414 LYS B 415
SITE 3 BC7 9 SER B 425
SITE 1 BC8 6 ARG B 40 ASP B 393 ASN B 396 EDO B 605
SITE 2 BC8 6 HOH B1038 HOH B1204
SITE 1 BC9 8 ASP B 354 GLY B 355 GLY B 384 PO4 B 604
SITE 2 BC9 8 HOH B 745 HOH B 790 HOH B 951 HOH B1000
SITE 1 CC1 7 LYS A 400 CYS A 401 PHE A 414 HIS B 247
SITE 2 CC1 7 SER B 248 THR B 251 HOH B 775
SITE 1 CC2 7 TYR A 195 ALA A 222 PHE B 9 ASN B 10
SITE 2 CC2 7 LEU B 13 ALA B 14 HOH B 901
CRYST1 60.511 106.799 83.040 90.00 96.59 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 0.016526 0.000000 0.001909 0.00000
SCALE2 0.000000 0.009363 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012122 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
